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  1 / 2959 MEDLINE  
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[PMID]:29362354
[Au] Autor:Garcia-Alai MM; Heidemann J; Skruzny M; Gieras A; Mertens HDT; Svergun DI; Kaksonen M; Uetrecht C; Meijers R
[Ad] Endereço:European Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
[Ti] Título:Epsin and Sla2 form assemblies through phospholipid interfaces.
[So] Source:Nat Commun;9(1):328, 2018 01 23.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Fúngicas/química
Fosfatidilinositol 4,5-Difosfato/química
Domínios Proteicos
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/genética
Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/genética
Membrana Celular/metabolismo
Chaetomium/genética
Chaetomium/metabolismo
Cristalografia por Raios X
Endocitose
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Seres Humanos
Modelos Moleculares
Fosfatidilinositol 4,5-Difosfato/metabolismo
Ligação Proteica
Multimerização Proteica
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Fungal Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (epsin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02443-x


  2 / 2959 MEDLINE  
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[PMID]:28468944
[Au] Autor:Montgomery DS; Yu L; Ghazi ZM; Thai TL; Al-Khalili O; Ma HP; Eaton DC; Alli AA
[Ad] Endereço:Department of Physiology and Functional Genomics and Department of Medicine Division of Nephrology, Hypertension, and Renal Transplantation, University of Florida College of Medicine, Gainesville, Florida.
[Ti] Título:ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins.
[So] Source:Am J Physiol Cell Physiol;313(1):C42-C53, 2017 Jul 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We previously demonstrated a role for the myristoylated alanine-rich C kinase substrate (MARCKS) to serve as an adaptor protein in the anionic phospholipid phosphate-dependent regulation of the epithelial sodium channel (ENaC). Both MARCKS and ENaC are regulated by proteolysis. Calpains are a family of ubiquitously expressed intracellular Ca -dependent cysteine proteases involved in signal transduction. Here we examine the role of calpain-2 in regulating MARCKS and ENaC in cultured renal epithelial cells and in the mouse kidney. Using recombinant fusion proteins, we show that MARCKS, but not the ENaC subunits, are a substrate of calpain-2 in the presence of Ca Pharmacological inhibition of calpain-2 alters MARCKS protein expression in light-density sucrose gradient fractions from cell lysates of mouse cortical collecting duct cells. Calpain-dependent cleaved products of MARCKS are detectable in cultured renal cells. Ca mobilization and calpain-2 inhibition decrease the association between ENaC and MARCKS. The inhibition of calpain-2 reduces ENaC activity as demonstrated by single-channel patch-clamp recordings and transepithelial current measurements. These results suggest that calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of ENaC activity in the kidney.
[Mh] Termos MeSH primário: Calpaína/genética
Canais Epiteliais de Sódio/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas de Membrana/genética
Fosfatidilinositol 4,5-Difosfato/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Amilorida/farmacologia
Animais
Cálcio/metabolismo
Calpaína/metabolismo
Fracionamento Celular
Linhagem Celular
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Inibidores de Cisteína Proteinase/farmacologia
Citocalasina D/farmacologia
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Canais Epiteliais de Sódio/metabolismo
Regulação da Expressão Gênica
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Túbulos Renais Coletores/citologia
Túbulos Renais Coletores/efeitos dos fármacos
Túbulos Renais Coletores/metabolismo
Proteínas de Membrana/metabolismo
Camundongos
Substrato Quinase C Rico em Alanina Miristoilada
Técnicas de Patch-Clamp
Proteólise/efeitos dos fármacos
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Transdução de Sinais
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cysteine Proteinase Inhibitors); 0 (Epithelial Sodium Channels); 0 (Intracellular Signaling Peptides and Proteins); 0 (Marcks protein, mouse); 0 (Membrane Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Recombinant Fusion Proteins); 125267-21-2 (Myristoylated Alanine-Rich C Kinase Substrate); 22144-77-0 (Cytochalasin D); 7DZO8EB0Z3 (Amiloride); EC 3.4.22.- (Calpain); EC 3.4.22.53 (Capn2 protein, mouse); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00244.2016


  3 / 2959 MEDLINE  
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[PMID]:29020060
[Au] Autor:Royal AA; Tinker A; Harmer SC
[Ad] Endereço:William Harvey Research Institute, The Heart Centre, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London, United Kingdom.
[Ti] Título:Phosphatidylinositol-4,5-bisphosphate is required for KCNQ1/KCNE1 channel function but not anterograde trafficking.
[So] Source:PLoS One;12(10):e0186293, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The slow delayed-rectifier potassium current (IKs) is crucial for human cardiac action potential repolarization. The formation of IKs requires co-assembly of the KCNQ1 α-subunit and KCNE1 ß-subunit, and mutations in either of these subunits can lead to hereditary long QT syndrome types 1 and 5, respectively. It is widely recognised that the KCNQ1/KCNE1 (Q1/E1) channel requires phosphatidylinositol-4,5-bisphosphate (PIP2) binding for function. We previously identified a cluster of basic residues in the proximal C-terminus of KCNQ1 that form a PIP2/phosphoinositide binding site. Upon charge neutralisation of these residues we found that the channel became more retained in the endoplasmic reticulum, which raised the possibility that channel-phosphoinositide interactions could play a role in channel trafficking. To explore this further we used a chemically induced dimerization (CID) system to selectively deplete PIP2 and/or phosphatidylinositol-4-phosphate (PI(4)P) at the plasma membrane (PM) or Golgi, and we subsequently monitored the effects on both channel trafficking and function. The depletion of PIP2 and/or PI(4)P at either the PM or Golgi did not alter channel cell-surface expression levels. However, channel function was extremely sensitive to the depletion of PIP2 at the PM, which is in contrast to the response of other cardiac potassium channels tested (Kir2.1 and Kv11.1). Surprisingly, when using the CID system IKs was dramatically reduced even before dimerization was induced, highlighting limitations regarding the utility of this system when studying processes highly sensitive to PIP2 depletion. In conclusion, we identify that the Q1/E1 channel does not require PIP2 or PI(4)P for anterograde trafficking, but is heavily reliant on PIP2 for channel function once at the PM.
[Mh] Termos MeSH primário: Canal de Potássio KCNQ1/metabolismo
Fosfatidilinositol 4,5-Difosfato/metabolismo
Canais de Potássio de Abertura Dependente da Tensão da Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Células CHO
Membrana Celular/efeitos dos fármacos
Membrana Celular/metabolismo
Cricetinae
Cricetulus
Retículo Endoplasmático/efeitos dos fármacos
Retículo Endoplasmático/metabolismo
Genes Reporter
Complexo de Golgi/efeitos dos fármacos
Complexo de Golgi/metabolismo
Células HEK293
Seres Humanos
Ativação do Canal Iônico/efeitos dos fármacos
Mutação/genética
Ligação Proteica/efeitos dos fármacos
Multimerização Proteica/efeitos dos fármacos
Transporte Proteico/efeitos dos fármacos
Sirolimo/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KCNE1 protein, human); 0 (KCNQ1 Potassium Channel); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Potassium Channels, Voltage-Gated); W36ZG6FT64 (Sirolimus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186293


  4 / 2959 MEDLINE  
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[PMID]:28945350
[Au] Autor:Hudson BN; Hyun SH; Thompson DH; Lyon AM
[Ad] Endereço:Department of Chemistry and ‡Department of Biological Sciences, Purdue University , West Lafayette, Indiana 47907, United States.
[Ti] Título:Phospholipase Cß3 Membrane Adsorption and Activation Are Regulated by Its C-Terminal Domains and Phosphatidylinositol 4,5-Bisphosphate.
[So] Source:Biochemistry;56(41):5604-5614, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipase Cß (PLCß) enzymes hydrolyze phosphatidylinositol 4,5-bisphosphate to produce second messengers that regulate intracellular Ca , cell proliferation, and survival. Their activity is dependent upon interfacial activation that occurs upon localization to cell membranes. However, the molecular basis for how these enzymes productively interact with the membrane is poorly understood. Herein, atomic force microscopy demonstrates that the ∼300-residue C-terminal domain promotes adsorption to monolayers and is required for spatial organization of the protein on the monolayer surface. PLCß variants lacking this C-terminal domain display differences in their distribution on the surface. In addition, a previously identified autoinhibitory helix that binds to the PLCß catalytic core negatively impacts membrane binding, providing an additional level of regulation for membrane adsorption. Lastly, defects in phosphatidylinositol 4,5-bisphosphate hydrolysis also alter monolayer adsorption, reflecting a role for the active site in this process. Together, these findings support a model in which multiple elements of PLCß modulate adsorption, distribution, and catalysis at the cell membrane.
[Mh] Termos MeSH primário: Bicamadas Lipídicas/metabolismo
Modelos Moleculares
Fosfatidilinositol 4,5-Difosfato/metabolismo
Fosfolipase C beta/metabolismo
[Mh] Termos MeSH secundário: Adsorção
Substituição de Aminoácidos
Domínio Catalítico
Ativação Enzimática
Estabilidade Enzimática
Fluorometria
Deleção de Genes
Seres Humanos
Hidrólise
Bicamadas Lipídicas/química
Lipossomos
Microscopia de Força Atômica
Mutagênese Sítio-Dirigida
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosfatidiletanolaminas/química
Fosfatidiletanolaminas/metabolismo
Fosfatidilinositol 4,5-Difosfato/química
Fosfolipase C beta/química
Fosfolipase C beta/genética
Mutação Puntual
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipid Bilayers); 0 (Liposomes); 0 (Peptide Fragments); 0 (Phosphatidylethanolamines); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Recombinant Fusion Proteins); EC 3.1.4.11 (PLCB3 protein, human); EC 3.1.4.11 (Phospholipase C beta)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00547


  5 / 2959 MEDLINE  
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[PMID]:28842476
[Au] Autor:Field SJ
[Ad] Endereço:From the Department of Medicine, Division of Endocrinology and Metabolism, University of California, San Diego, La Jolla, California 92093 sjfield@ucsd.edu.
[Ti] Título:Spelunking for lipids in caveolae.
[So] Source:J Biol Chem;292(34):14308-14309, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphatidylserine (PtdSer) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P ) have been implicated in the maintenance of caveolae, but direct evidence that these lipids are required for normal caveolar structure and dynamics in living cells has been lacking. A new study by Fairn and colleagues uses sophisticated tools to perturb specific lipids in living cells to assess the consequences for caveolae. This study demonstrates disparate roles for these lipids in the stability and mobility of caveolae and points the way for future work to understand how these lipids contribute to the biology of caveolae.
[Mh] Termos MeSH primário: Cavéolas/metabolismo
Membrana Celular/metabolismo
Fosfatidilinositol 4,5-Difosfato/metabolismo
Fosfatidilserinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Cavéolas/química
Caveolinas/química
Caveolinas/metabolismo
Membrana Celular/química
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/química
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas Musculares/química
Proteínas Musculares/metabolismo
Fosfatidilinositol 4,5-Difosfato/química
Fosfatidilserinas/química
Multimerização Proteica
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Caveolins); 0 (Intracellular Signaling Peptides and Proteins); 0 (MURC protein, human); 0 (Muscle Proteins); 0 (PRKCDBP protein, human); 0 (PTRF protein, human); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Phosphatidylserines); 0 (RNA-Binding Proteins); 0 (SDPR protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.H117.791400


  6 / 2959 MEDLINE  
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[PMID]:28698382
[Au] Autor:Hirama T; Das R; Yang Y; Ferguson C; Won A; Yip CM; Kay JG; Grinstein S; Parton RG; Fairn GD
[Ad] Endereço:From the Keenan Research Centre for Biomedical Science, St. Michael's Hospital, Toronto, Ontario M5B 1W8, Canada.
[Ti] Título:Phosphatidylserine dictates the assembly and dynamics of caveolae in the plasma membrane.
[So] Source:J Biol Chem;292(34):14292-14307, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Caveolae are bulb-shaped nanodomains of the plasma membrane that are enriched in cholesterol and sphingolipids. They have many physiological functions, including endocytic transport, mechanosensing, and regulation of membrane and lipid transport. Caveola formation relies on integral membrane proteins termed caveolins (Cavs) and the cavin family of peripheral proteins. Both protein families bind anionic phospholipids, but the precise roles of these lipids are unknown. Here, we studied the effects of phosphatidylserine (PtdSer), phosphatidylinositol 4-phosphate (PtdIns4P), and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P ) on caveolar formation and dynamics. Using live-cell, single-particle tracking of GFP-labeled Cav1 and ultrastructural analyses, we compared the effect of PtdSer disruption or phosphoinositide depletion with caveola disassembly caused by cavin1 loss. We found that PtdSer plays a crucial role in both caveola formation and stability. Sequestration or depletion of PtdSer decreased the number of detectable Cav1-GFP puncta and the number of caveolae visualized by electron microscopy. Under PtdSer-limiting conditions, the co-localization of Cav1 and cavin1 was diminished, and cavin1 degradation was increased. Using rapamycin-recruitable phosphatases, we also found that the acute depletion of PtdIns4P and PtdIns(4,5)P has minimal impact on caveola assembly but results in decreased lateral confinement. Finally, we show in a model of phospholipid scrambling, a feature of apoptotic cells, that caveola stability is acutely affected by the scrambling. We conclude that the predominant plasmalemmal anionic lipid PtdSer is essential for proper Cav clustering, caveola formation, and caveola dynamics and that membrane scrambling can perturb caveolar stability.
[Mh] Termos MeSH primário: Cavéolas/metabolismo
Caveolina 1/metabolismo
Membrana Celular/metabolismo
Modelos Biológicos
Fosfatidilserinas/metabolismo
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Cavéolas/química
Cavéolas/ultraestrutura
Caveolina 1/antagonistas & inibidores
Caveolina 1/química
Caveolina 1/genética
Linhagem Celular
Membrana Celular/química
Membrana Celular/ultraestrutura
Rastreamento de Células
Cricetulus
Seres Humanos
Cinética
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Mesocricetus
Microscopia Eletrônica de Transmissão
Microscopia de Vídeo
Fosfatidilinositol 4,5-Difosfato/química
Fosfatidilinositol 4,5-Difosfato/metabolismo
Fosfatos de Fosfatidilinositol/química
Fosfatos de Fosfatidilinositol/metabolismo
Fosfatidilserinas/química
Transporte Proteico
Interferência de RNA
Proteínas de Ligação a RNA/antagonistas & inibidores
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CAV1 protein, human); 0 (Caveolin 1); 0 (Luminescent Proteins); 0 (PTRF protein, human); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Phosphatidylinositol Phosphates); 0 (Phosphatidylserines); 0 (RNA-Binding Proteins); 0 (Recombinant Fusion Proteins); 0 (phosphatidylinositol 4-phosphate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.791400


  7 / 2959 MEDLINE  
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[PMID]:28676499
[Au] Autor:Maheshwari S; Miller MS; O'Meally R; Cole RN; Amzel LM; Gabelli SB
[Ad] Endereço:From the Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
[Ti] Título:Kinetic and structural analyses reveal residues in phosphoinositide 3-kinase α that are critical for catalysis and substrate recognition.
[So] Source:J Biol Chem;292(33):13541-13550, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphoinositide 3-kinases (PI3Ks) are ubiquitous lipid kinases that activate signaling cascades controlling cell survival, proliferation, protein synthesis, and vesicle trafficking. PI3Ks have dual kinase specificity: a lipid kinase activity that phosphorylates the 3'-hydroxyl of phosphoinositides and a protein-kinase activity that includes autophosphorylation. Despite the wealth of biochemical and structural information on PI3Kα, little is known about the identity and roles of individual active-site residues in catalysis. To close this gap, we explored the roles of residues of the catalytic domain and the regulatory subunit of human PI3Kα in lipid and protein phosphorylation. Using site-directed mutagenesis, kinetic assays, and quantitative mass spectrometry, we precisely mapped key residues involved in substrate recognition and catalysis by PI3Kα. Our results revealed that Lys-776, located in the P-loop of PI3Kα, is essential for the recognition of lipid and ATP substrates and also plays an important role in PI3Kα autophosphorylation. Replacement of the residues His-936 and His-917 in the activation and catalytic loops, respectively, with alanine dramatically changed PI3Kα kinetics. Although H936A inactivated the lipid kinase activity without affecting autophosphorylation, H917A abolished both the lipid and protein kinase activities of PI3Kα. On the basis of these kinetic and structural analyses, we propose possible mechanistic roles of these critical residues in PI3Kα catalysis.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Modelos Moleculares
Fosfatidilinositol 3-Quinases/metabolismo
Fosfatidilinositol 4,5-Difosfato/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Substituição de Aminoácidos
Sítios de Ligação
Biocatálise
Domínio Catalítico
Classe I de Fosfatidilinositol 3-Quinases
Histidina/química
Histidina/metabolismo
Seres Humanos
Cinética
Lisina/química
Lisina/metabolismo
Conformação Molecular
Mutagênese Sítio-Dirigida
Fosfatidilinositol 3-Quinases/química
Fosfatidilinositol 3-Quinases/genética
Fosfatidilinositol 4,5-Difosfato/química
Fosforilação
Mutação Puntual
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphatidylinositol 4,5-Diphosphate); 4QD397987E (Histidine); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (PIK3R1 protein, human); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (Class I Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (PIK3CA protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.772426


  8 / 2959 MEDLINE  
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[PMID]:28634262
[Au] Autor:Dickson EJ
[Ad] Endereço:Department of Physiology and Membrane Biology, School of Medicine, University of California Davis, Davis, CA ejdickson@ucdavis.edu.
[Ti] Título:RASSF4: Regulator of plasma membrane PI(4,5)P .
[So] Source:J Cell Biol;216(7):1879-1881, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P ) is a negatively charged phospholipid that plays a major role in recruiting and regulating proteins at the plasma membrane-cytosol interface. In this issue, Chen et al. (2017. https://doi.org/10.1083/jcb.201606047) demonstrate that RAS association domain family 4 (RASSF4) positively influences PI(4,5)P synthesis through ARF6-dependent regulation of PIP5K.
[Mh] Termos MeSH primário: Membrana Celular
Fosfatidilinositol 4,5-Difosfato
[Mh] Termos MeSH secundário: Fosfatidilinositóis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphatidylinositol 4,5-Diphosphate); 0 (Phosphatidylinositols)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201706042


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[PMID]:28600435
[Au] Autor:Chen YJ; Chang CL; Lee WR; Liou J
[Ad] Endereço:Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX.
[Ti] Título:RASSF4 controls SOCE and ER-PM junctions through regulation of PI(4,5)P .
[So] Source:J Cell Biol;216(7):2011-2025, 2017 Jul 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RAS association domain family 4 (RASSF4) is involved in tumorigenesis and regulation of the Hippo pathway. In this study, we identify new functional roles of RASSF4. First, we discovered that RASSF4 regulates store-operated Ca entry (SOCE), a fundamental Ca signaling mechanism, by affecting the translocation of the endoplasmic reticulum (ER) Ca sensor stromal interaction molecule 1 (STIM1) to ER-plasma membrane (PM) junctions. It was further revealed that RASSF4 regulates the formation of ER-PM junctions and the ER-PM tethering function of extended synaptotagmins E-Syt2 and E-Syt3. Moreover, steady-state PM phosphatidylinositol 4,5-bisphosphate (PI[4,5]P ) levels, important for localization of STIM1 and E-Syts at ER-PM junctions, were reduced in -knockdown cells. Furthermore, we demonstrated that RASSF4 interacts with and regulates the activity of adenosine diphosphate ribosylation factor 6 (ARF6), a small G protein and upstream regulator of type I phosphatidylinositol phosphate kinases (PIP5Ks) and PM PI(4,5)P levels. Overall, our study suggests that RASSF4 controls SOCE and ER-PM junctions through ARF6-dependent regulation of PM PI(4,5)P levels, pivotal for a variety of physiological processes.
[Mh] Termos MeSH primário: Sinalização do Cálcio
Membrana Celular/metabolismo
Retículo Endoplasmático/metabolismo
Proteínas de Neoplasias/metabolismo
Proteína ORAI1/metabolismo
Fosfatidilinositol 4,5-Difosfato/metabolismo
Molécula 1 de Interação Estromal/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/genética
Fatores de Ribosilação do ADP/metabolismo
Feminino
Células HeLa
Seres Humanos
Microscopia de Fluorescência
Microscopia de Vídeo
Proteínas de Neoplasias/genética
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Transporte Proteico
Interferência de RNA
Molécula 1 de Interação Estromal/genética
Sinaptotagmina II/genética
Sinaptotagmina II/metabolismo
Sinaptotagminas/genética
Sinaptotagminas/metabolismo
Fatores de Tempo
Imagem com Lapso de Tempo
Transfecção
Proteínas Supressoras de Tumor/genética
Neoplasias do Colo do Útero/genética
Neoplasias do Colo do Útero/metabolismo
Neoplasias do Colo do Útero/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (RASSF4 protein, human); 0 (STIM1 protein, human); 0 (SYT2 protein, human); 0 (SYT3 protein, human); 0 (Stromal Interaction Molecule 1); 0 (Synaptotagmin II); 0 (Tumor Suppressor Proteins); 134193-27-4 (Synaptotagmins); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.68 (1-phosphatidylinositol-4-phosphate 5-kinase); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ADP-ribosylation factor 6)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170611
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201606047


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[PMID]:28542408
[Au] Autor:Li L; Chen X; Zhang S; Yang J; Chen D; Liu M; Zhang H; Zheng X; Wang P; Peng Y; Zhang Z
[Ad] Endereço:Department of Plant Pathology, College of Plant Protection, Nanjing Agricultural University, and Key Laboratory of Integrated Management of Crop Diseases and Pests, Ministry of Education, Nanjing, China.
[Ti] Título:MoCAP proteins regulated by MoArk1-mediated phosphorylation coordinate endocytosis and actin dynamics to govern development and virulence of Magnaporthe oryzae.
[So] Source:PLoS Genet;13(5):e1006814, 2017 May.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Actin organization is a conserved cellular process that regulates the growth and development of eukaryotic cells. It also governs the virulence process of pathogenic fungi, such as the rice blast fungus Magnaporthe oryzae, with mechanisms not yet fully understood. In a previous study, we found that actin-regulating kinase MoArk1 displays conserved functions important in endocytosis and actin organization, and MoArk1 is required for maintaining the growth and full virulence of M. oryzae. To understand how MoArk1 might function, we identified capping protein homologs from M. oryzae (MoCAP) that interact with MoArk1 in vivo. MoCAP is heterodimer consisting of α and ß subunits MoCapA and MoCapB. Single and double deletions of MoCAP subunits resulted in abnormal mycelial growth and conidia formation. The ΔMocap mutants also exhibited reduced appressorium penetration and invasive hyphal growth within host cells. Furthermore, the ΔMocap mutants exhibited delayed endocytosis and abnormal cytoskeleton assembly. Consistent with above findings, MoCAP proteins interacted with MoAct1, co-localized with actin during mycelial development, and participated in appressorial actin ring formation. Further analysis revealed that the S85 residue of MoCapA and the S285 residue of MoCapB were subject to phosphorylation by MoArk1 that negatively regulates MoCAP functions. Finally, the addition of exogenous phosphatidylinositol 4,5-bisphosphate (PIP2) failed to modulate actin ring formation in ΔMocap mutants, in contrast to the wild-type strain, suggesting that MoCAP may also mediate phospholipid signaling in the regulation of the actin organization. These results together demonstrate that MoCAP proteins whose functions are regulated by MoArk1 and PIP2 are important for endocytosis and actin dynamics that are directly linked to growth, conidiation and pathogenicity of M. oryzae.
[Mh] Termos MeSH primário: Proteínas de Capeamento de Actina/metabolismo
Actinas/metabolismo
Endocitose
Proteínas Fúngicas/metabolismo
Magnaporthe/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Capeamento de Actina/genética
Magnaporthe/crescimento & desenvolvimento
Magnaporthe/patogenicidade
Micélio/crescimento & desenvolvimento
Fosfatidilinositol 4,5-Difosfato/metabolismo
Fosforilação
Proteínas Serina-Treonina Quinases/genética
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actin Capping Proteins); 0 (Actins); 0 (Fungal Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006814



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