p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins
about
Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transportThe Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31ABiochemical and molecular characterization of two phosphatidic acid-selective phospholipase A1s, mPA-PLA1alpha and mPA-PLA1betaPhosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamicsAssembly, organization, and function of the COPII coatSec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cellsVesicle-mediated export from the ER: COPII coat function and regulationPhospholipases of mineralization competent cells and matrix vesicles: roles in physiological and pathological mineralizationsPhospholipases A₁A membrane protein enriched in endoplasmic reticulum exit sites interacts with COPIIp125/Sec23-interacting protein (Sec23ip) is required for spermiogenesisThe hereditary spastic paraplegia-related enzyme DDHD2 is a principal brain triglyceride lipaseBeta-catenin asymmetry is regulated by PLA1 and retrograde traffic in C. elegans stem cell divisions.Intracellular phospholipase A1gamma (iPLA1gamma) is a novel factor involved in coat protein complex I- and Rab6-independent retrograde transport between the endoplasmic reticulum and the Golgi complexMapping of functional domains of gamma-SNAP.Hereditary spastic paraplegia: clinico-pathologic features and emerging molecular mechanisms.Phosphatidic acid phospholipase A1 mediates ER-Golgi transit of a family of G protein-coupled receptors.Large-scale profiling of Rab GTPase trafficking networks: the membrome.p125A exists as part of the mammalian Sec13/Sec31 COPII subcomplex to facilitate ER-Golgi transport.Lipid metabolism and regulation of membrane trafficking.Alteration of fatty-acid-metabolizing enzymes affects mitochondrial form and function in hereditary spastic paraplegia.p125 is localized in endoplasmic reticulum exit sites and involved in their organization.Mammalian Sec16/p250 plays a role in membrane traffic from the endoplasmic reticulum.The metabolic serine hydrolases and their functions in mammalian physiology and disease.Mutations in DDHD2, encoding an intracellular phospholipase A(1), cause a recessive form of complex hereditary spastic paraplegia.A novel phospholipase from Trypanosoma bruceiMutations in phospholipase DDHD2 cause autosomal recessive hereditary spastic paraplegia (SPG54).ER exit sites--localization and control of COPII vesicle formation.A cascade of ER exit site assembly that is regulated by p125A and lipid signals.Emergent properties of proteostasis-COPII coupled systems in human health and disease.A PLA1-2 punch regulates the Golgi complex.14-3-3 protein and ATRAP bind to the soluble class IIB phosphatidylinositol transfer protein RdgBβ at distinct sites.A novel phospholipase A1 with sequence homology to a mammalian Sec23p-interacting protein, p125.Surface loops of extracellular phospholipase A(1) determine both substrate specificity and preference for lysophospholipids.Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export.Dual function of Sec16B: Endoplasmic reticulum-derived protein secretion and peroxisome biogenesis in mammalian cells.The mammalian protein-protein interaction database and its viewing system that is linked to the main FANTOM2 viewer.The main triglyceride-lipase from the insect fat body is an active phospholipase A(1): identification and characterization.Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species.TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER-Golgi intermediate compartments.
P2860
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P2860
p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@ast
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en-gb
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@nl
type
label
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@ast
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en-gb
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@nl
prefLabel
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@ast
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en-gb
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@nl
P2093
P2860
P356
P1476
p125 is a novel mammalian Sec2 ...... hospholipid-modifying proteins
@en
P2093
P2860
P304
P356
10.1074/JBC.274.29.20505
P407
P577
1999-07-16T00:00:00Z