GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking - Wikidata - wikimedia - TriplyDB

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

http://www.wikidata.org/entity/Q33615083

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VAMP4 is required to maintain the ribbon structure of the Golgi apparatus The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning GRASP: A Multitasking Tether Mechanisms and Regulation of the Mitotic Inheritance of the Golgi Complex GRASPs in Golgi Structure and Function Golgi Fragmentation in ALS Motor Neurons. New Mechanisms Targeting Microtubules, Tethers, and Transport Vesicles Golgi fragmentation in Alzheimer's disease Golgi defects enhance APP amyloidogenic processing in Alzheimer's disease C11ORF24 is a novel type I membrane protein that cycles between the Golgi apparatus and the plasma membrane in Rab6-positive vesicles Phosphorylation of Golgi Peripheral Membrane Protein Grasp65 Is an Integral Step in the Formation of the Human Cytomegalovirus Cytoplasmic Assembly Compartment Structural Insight into Golgi Membrane Stacking by GRASP65 and GRASP55 Proteins The Golgi complex in stress and death The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis.Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization.Epithelial-to-mesenchymal transition drives a pro-metastatic Golgi compaction process through scaffolding protein PAQR11.Signaling at the Golgi during mitosis.Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics.Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis.Are Rab proteins the link between Golgi organization and membrane trafficking?Dual anchoring of the GRASP membrane tether promotes trans pairing Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V.Golgi compartmentation and identity.cPLA2 is protective against COX inhibitor-induced intestinal damage.Unraveling the Golgi ribbon New components of the Golgi matrix.Golgi complex fragmentation in G2/M transition: An organelle-based cell-cycle checkpoint.Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligand Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130.Golgi biogenesis The golgin coiled-coil proteins of the Golgi apparatus.Cell cycle regulation of VCIP135 deubiquitinase activity and function in p97/p47-mediated Golgi reassembly.The role of GRASP65 in Golgi cisternal stacking and cell cycle progression.Reconstitution of the cell cycle-regulated Golgi disassembly and reassembly in a cell-free system.Modular organization of the mammalian Golgi apparatus Mena-GRASP65 interaction couples actin polymerization to Golgi ribbon linking Functional Characterization of Monomeric GTPase Rab1 in the Secretory Pathway of Leishmania Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly.

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P2860

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

http://www.wikidata.org/entity/Q33615083

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@ast

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@en

type

label

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@ast

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@en

prefLabel

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@ast

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@en

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P2860

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P1433

Journal of Cell Biology

P1476

GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking

@en

P2093

Yanzhuang Wang

http://www.w3.org/2001/XMLSchema#string

Yi Xiang

http://www.w3.org/2001/XMLSchema#string

P2860

A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic

The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation

GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution

The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53, and p25 are required to maintain the architecture of ERGIC and Golgi.

The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division

GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.

Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55

Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2

The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis

Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2

P304

237-251

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scholarly article

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10.1083/JCB.200907132

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P433

2

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188

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2010-01-18T00:00:00Z

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41056231

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20083603

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2812519

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