ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner
about
The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membraneIdentification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutantsVPS37 isoforms differentially modulate the ternary complex formation of ALIX, ALG-2, and ESCRT-IAssembly, organization, and function of the COPII coatMultifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane TraffickingVesicle-mediated export from the ER: COPII coat function and regulationVesicle-mediated ER export of proteins and lipidsMolecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognitionThe yeast penta-EF protein Pef1p is involved in cation-dependent budding and cell polarization.The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) proteinStructural and Functional Study of Apoptosis-linked Gene-2·Heme-binding Protein 2 Interactions in HIV-1 ProductionStructural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.Vesicular calcium regulates coat retention, fusogenicity, and size of pre-Golgi intermediates.Modulation of the secretory pathway rescues zebrafish polycystic kidney disease pathology.Apoptosis-linked gene-2 (ALG-2)/Sec31 interactions regulate endoplasmic reticulum (ER)-to-Golgi transport: a potential effector pathway for luminal calciumMechanism of Ca²⁺-triggered ESCRT assembly and regulation of cell membrane repair.A new role for annexin A11 in the early secretory pathway via stabilizing Sec31A protein at the endoplasmic reticulum exit sites (ERES)PDCD6 is an independent predictor of progression free survival in epithelial ovarian cancerPenta-EF-Hand Protein Peflin Is a Negative Regulator of ER-To-Golgi Transport.Variations in the PDCD6 gene are associated with increased uterine leiomyoma risk in the Chinese.Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1.ER exit sites--localization and control of COPII vesicle formation.Structure and function of ALG-2, a penta-EF-hand calcium-dependent adaptor protein.COPII and the regulation of protein sorting in mammals.Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum.Endoplasmic reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs.ALG-2-interacting Tubby-like protein superfamily member PLSCR3 is secreted by an exosomal pathway and taken up by recipient cultured cells.Brox, a novel farnesylated Bro1 domain-containing protein that associates with charged multivesicular body protein 4 (CHMP4).The apoptosis linked gene ALG-2 is dysregulated in tumors of various origin and contributes to cancer cell viability.Nuclear ALG-2 protein interacts with Ca2+ homeostasis endoplasmic reticulum protein (CHERP) Ca2+-dependently and participates in regulation of alternative splicing of inositol trisphosphate receptor type 1 (IP3R1) pre-mRNA.Prediction of a new ligand-binding site for type 2 motif based on the crystal structure of ALG-2 by dry and wet approaches.Identification of Cysteine Ubiquitylation Sites on the Sec23A Protein of the COPII Complex Required for Vesicle Formation from the ER.The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins.Mutations in the vesicular trafficking protein annexin A11 are associated with amyotrophic lateral sclerosis.Nanoluciferase Reporter Gene System Directed by Tandemly Repeated Pseudo-Palindromic NFAT-Response Elements Facilitates Analysis of Biological Endpoint Effects of Cellular Ca2+ Mobilization.The ALG-2 binding site in Sec31A influences the retention kinetics of Sec31A at the endoplasmic reticulum exit sites as revealed by live-cell time-lapse imaging.
P2860
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P248
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P2860
ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@ast
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en-gb
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@nl
type
label
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@ast
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en-gb
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@nl
prefLabel
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@ast
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en-gb
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@nl
P2093
P921
P3181
P1476
ALG-2 directly binds Sec31A an ...... tes in a Ca2+-dependent manner
@en
P2093
Haruna Yoshida
Hideki Shibata
Hironori Suzuki
Masatoshi Maki
P304
P3181
P356
10.1016/J.BBRC.2006.12.101
P407
P577
2007-02-16T00:00:00Z