Mapping the functional domains of the Golgi stacking factor GRASP65 - Wikidata - awgldk - TriplyDB

Mapping the functional domains of the Golgi stacking factor GRASP65

Mapping the functional domains of the Golgi stacking factor GRASP65

http://www.wikidata.org/entity/Q28296248

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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 The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division ZFPL1, a novel ring finger protein required for cis-Golgi integrity and efficient ER-to-Golgi transport The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis GRASP: A Multitasking Tether Mechanisms and Regulation of the Mitotic Inheritance of the Golgi Complex GRASPs in Golgi Structure and Function Golgi fragmentation in Alzheimer's disease Golgi defects enhance APP amyloidogenic processing in Alzheimer's disease Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane Tethering Allosteric Regulation of GRASP Protein-dependent Golgi Membrane Tethering by Mitotic Phosphorylation Structural Insight into Golgi Membrane Stacking by GRASP65 and GRASP55 Proteins Convergence of cell cycle regulation and growth factor signals on GRASP65 GMx33 associates with the trans-Golgi matrix in a dynamic manner and sorts within tubules exiting the Golgi.GRASP65 controls the cis Golgi integrity in vivo.The kinetics of G2 and M transitions regulated by B cyclins Ordered assembly of the duplicating Golgi in Trypanosoma brucei.GRASP55 regulates Golgi ribbon formation.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.Direct selection of monoclonal phosphospecific antibodies without prior phosphoamino acid mapping.Direct observation of molecular arrays in the organized smooth endoplasmic reticulum.Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly and reassembly GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking Dual anchoring of the GRASP membrane tether promotes trans pairing Golgi compartmentation and identity.Unraveling the Golgi ribbon New components of the Golgi matrix.Golgi partitioning controls mitotic entry through Aurora-A kinase.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 Golgi biogenesis 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.The role of Golgi reassembly and stacking protein 65 phosphorylation in H2O2-induced cell death and Golgi morphological changes.

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P2860

Mapping the functional domains of the Golgi stacking factor GRASP65

http://www.wikidata.org/entity/Q28296248

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2005年の論文

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2005年論文

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2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Mapping the functional domains of the Golgi stacking factor GRASP65

@ast

Mapping the functional domains of the Golgi stacking factor GRASP65

@en

Mapping the functional domains of the Golgi stacking factor GRASP65

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type

label

Mapping the functional domains of the Golgi stacking factor GRASP65

@ast

Mapping the functional domains of the Golgi stacking factor GRASP65

@en

Mapping the functional domains of the Golgi stacking factor GRASP65

@nl

prefLabel

Mapping the functional domains of the Golgi stacking factor GRASP65

@ast

Mapping the functional domains of the Golgi stacking factor GRASP65

@en

Mapping the functional domains of the Golgi stacking factor GRASP65

@nl

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P3181

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P1433

Journal of Biological Chemistry

P1476

Mapping the functional domains of the Golgi stacking factor GRASP65

@en

P2093

Ayano Satoh

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

Graham Warren

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

Yanzhuang Wang

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

P2860

Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae

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

Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis

A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis

A direct role for GRASP65 as a mitotically regulated Golgi stacking factor

Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus

The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

GRASP65, a protein involved in the stacking of Golgi cisternae

The Golgi apparatus: 100 years of progress and controversy

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4921-8

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scholarly article

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4483128

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10.1074/JBC.M412407200

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6

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280

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