Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells
about
A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transportExophilin4/Slp2-a targets glucagon granules to the plasma membrane through unique Ca2+-inhibitory phospholipid-binding activity of the C2A domainThe Rab27a-binding protein, JFC1, regulates androgen-dependent secretion of prostate-specific antigen and prostatic-specific acid phosphataseGranuphilin modulates the exocytosis of secretory granules through interaction with syntaxin 1aThe Rab27a/granuphilin complex regulates the exocytosis of insulin-containing dense-core granulesMutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden miceNoc2 is essential in normal regulation of exocytosis in endocrine and exocrine cellsRegulation of vesicular trafficking and leukocyte function by Rab27 GTPases and their effectorsGranuphilin exclusively mediates functional granule docking to the plasma membrane.Structural basis of cargo recognitions for class V myosinsSlac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transportSlp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cellsThe Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domainMicroRNA-9 controls the expression of Granuphilin/Slp4 and the secretory response of insulin-producing cellsA subset of p23 localized on secretory granules in pancreatic beta-cellsNeurexin-1α contributes to insulin-containing secretory granule dockingSlac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actinMyosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cellsThe Rab27a effector exophilin7 promotes fusion of secretory granules that have not been docked to the plasma membrane.The Drosophila synaptotagmin-like protein bitesize is required for growth and has mRNA localization sequences within its open reading frame.The role of Rab3a in secretory vesicle docking requires association/dissociation of guanidine phosphates and Munc18-1.Rab27a mediates the tight docking of insulin granules onto the plasma membrane during glucose stimulation.Pancreatic beta-cell protein granuphilin binds Rab3 and Munc-18 and controls exocytosis.Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions.Slp4-a/granuphilin-a regulates dense-core vesicle exocytosis in PC12 cells.Synaptotagmin-like protein (Slp) homology domain 1 of Slac2-a/melanophilin is a critical determinant of GTP-dependent specific binding to Rab27A.Melanophilin, the product of the leaden locus, is required for targeting of myosin-Va to melanosomes.PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis.Whole exome sequencing in females with autism implicates novel and candidate genes.Modular genetic control of sexually dimorphic behaviors.Involvement of the Rab27 binding protein Slac2c/MyRIP in insulin exocytosis.Granuphilin molecularly docks insulin granules to the fusion machinery.Contrasting patterns of expression of transcription factors in pancreatic alpha and beta cells.Secretory vesicle docking to the plasma membrane: molecular mechanism and functional significance.Novel aspects of the molecular mechanisms controlling insulin secretion.More than just a cargo adapter, melanophilin prolongs and slows processive runs of myosin VaMolecular medicine of microRNAs: structure, function and implications for diabetes.Characterization of the mouse pancreatic islet proteome and comparative analysis with other mouse tissues.Mechanisms of biphasic insulin-granule exocytosis - roles of the cytoskeleton, small GTPases and SNARE proteins.The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical calcium-dependent phospholipid-binding machine: comparison with the C2A domain of synaptotagmin I.
P2860
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P2860
Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells
description
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im Oktober 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/10/01)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/10/01)
@nl
наукова стаття, опублікована в жовтні 1999
@uk
name
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@ast
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@en
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@nl
type
label
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@ast
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@en
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@nl
prefLabel
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@ast
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@en
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@nl
P2093
P2860
P3181
P356
P1476
Novel rabphilin-3-like protein ...... nules in pancreatic beta cells
@en
P2093
P2860
P304
28542–28548
P3181
P356
10.1074/JBC.274.40.28542
P407
P577
1999-10-01T00:00:00Z