GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.
about
A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expressionA GRASP55-rab2 effector complex linking Golgi structure to membrane trafficStructure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesisAn OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterningYSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zetaA role of histone H3 lysine 4 methyltransferase components in endosomal traffickingFunctional dissection of Rab GTPases involved in primary cilium formationGolgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogenDymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a protein integral to extracellular matrix and golgi organization and is associated with protein secretion pathways critical in bone developmentPolo-like kinase is required for the fragmentation of pericentriolar Golgi stacks during mitosisTransmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosisA direct role for GRASP65 as a mitotically regulated Golgi stacking factorGolgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatusPhosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragmentsSpatial partitioning of secretory cargo from Golgi resident proteins in live cells.GRASP: A Multitasking TetherGRASPs in Golgi Structure and FunctionGolgi fragmentation in Alzheimer's diseaseProtein kinase A activity is necessary for fission and fusion of Golgi to endoplasmic reticulum retrograde tubulesDistinct Biochemical Pools of Golgi Phosphoprotein 3 in the Human Breast Cancer Cell Lines MCF7 and MDA-MB-231Pentameric Assembly of Potassium Channel Tetramerization Domain-Containing Protein 5Structural Insight into Golgi Membrane Stacking by GRASP65 and GRASP55 ProteinsThe yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi trafficAdy4p and Spo74p are components of the meiotic spindle pole body that promote growth of the prospore membrane in Saccharomyces cerevisiae.The CORVET subunit Vps8 cooperates with the Rab5 homolog Vps21 to induce clustering of late endosomal compartments.Golgin-84 is a rab1 binding partner involved in Golgi structureTAPAS-1, a novel microdomain within the unique N-terminal region of the PDE4A1 cAMP-specific phosphodiesterase that allows rapid, Ca2+-triggered membrane association with selectivity for interaction with phosphatidic acidConvergence of cell cycle regulation and growth factor signals on GRASP65Mapping the functional domains of the Golgi stacking factor GRASP65GMx33 associates with the trans-Golgi matrix in a dynamic manner and sorts within tubules exiting the Golgi.Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1βGRASP65 controls the cis Golgi integrity in vivo.Cis-Golgi matrix proteins move directly to endoplasmic reticulum exit sites by association with tubules.GRASP55 regulates Golgi ribbon formation.The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.The Golgi protein p115 associates with gamma-tubulin and plays a role in Golgi structure and mitosis progression.Dynein light chain 1 and a spindle-associated adaptor promote dynein asymmetry and spindle orientation.
P2860
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P2860
GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին 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
GRASP55, a second mammalian GR ...... isternae in a cell-free system
@nl
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@ast
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en-gb
type
label
GRASP55, a second mammalian GR ...... isternae in a cell-free system
@nl
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@ast
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en-gb
prefLabel
GRASP55, a second mammalian GR ...... isternae in a cell-free system
@nl
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@ast
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en
GRASP55, a second mammalian GR ...... sternae in a cell-free system.
@en-gb
P2093
P50
P3181
P356
P1433
P1476
GRASP55, a second mammalian GR ...... isternae in a cell-free system
@en
P2093
P304
P3181
P356
10.1093/EMBOJ/18.18.4949
P407
P577
1999-09-01T00:00:00Z