The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A - Test2 - elhamkhani - TriplyDB

The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A

The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A

http://www.wikidata.org/entity/Q24301704

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The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane Identification 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 mutants Assembly, organization, and function of the COPII coat Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking Determinants of Glycosaminoglycan (GAG) Structure Vesicle-mediated export from the ER: COPII coat function and regulation Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex.The yeast penta-EF protein Pef1p is involved in cation-dependent budding and cell polarization.Involvement of the penta-EF-hand protein Pef1p in the Ca2+-dependent regulation of COPII subunit assembly in Saccharomyces cerevisiae.The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein Structural and Functional Study of Apoptosis-linked Gene-2·Heme-binding Protein 2 Interactions in HIV-1 Production Structural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2 ALG-2 attenuates COPII budding in vitro and stabilizes the Sec23/Sec31A complex.Annexins as Overlooked Regulators of Membrane Trafficking in Plant Cells 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 calcium CK2 phosphorylates Sec31 and regulates ER-To-Golgi trafficking A new role for annexin A11 in the early secretory pathway via stabilizing Sec31A protein at the endoplasmic reticulum exit sites (ERES)Calcium: a fundamental regulator of intracellular membrane fusion?Penta-EF-Hand Protein Peflin Is a Negative Regulator of ER-To-Golgi Transport.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.Apoptosis-linked gene 2 promotes breast cancer growth and metastasis by regulating the cytoskeleton.Emergent properties of proteostasis-COPII coupled systems in human health and disease.Structure and function of ALG-2, a penta-EF-hand calcium-dependent adaptor protein.COPII and the regulation of protein sorting in mammals.Insights from human congenital disorders of intestinal lipid metabolism.Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum.Deregulated ALG-2/HEBP2 axis alters microtubule dynamics and mitotic spindle behavior to stimulate cancer development.The apoptosis linked gene ALG-2 is dysregulated in tumors of various origin and contributes to cancer cell viability.COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments 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.Mammalian TRAPPIII Complex positively modulates the recruitment of Sec13/31 onto COPII vesicles.Host endoplasmic reticulum COPII proteins control cell-to-cell spread of the bacterial pathogen Listeria monocytogenes.The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins.Sr2+ has low efficiency in regulating spontaneous release at the Calyx of Held synapses.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.Association of PDCD6 polymorphisms with the risk of cancer: Evidence from a meta-analysis.

P2860

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P2860

The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A

http://www.wikidata.org/entity/Q24301704

description

2006 nî lūn-bûn

@nan

2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

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MBC.E06-05-0444

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Molecular Biology of the Cell

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The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A

@en

P2093

Akinori Yamasaki

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

Akitsugu Yamamoto

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

Katsuko Tani

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

Masayuki Komada

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

Naomi Kitamura

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

P2860

p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins

Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport

Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner

The protein network of HIV budding

The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting

The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1

Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3

The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner

The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B

Brefeldin A: insights into the control of membrane traffic and organelle structure

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scholarly article

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938767

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10.1091/MBC.E06-05-0444

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P433

11

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17

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2006-11-01T00:00:00Z

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237739752

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16957052

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P921

endoplasmic reticulum exit site

Programmed cell death 6

Programmed cell death 6 interacting protein

SEC31 homolog A, COPII coat complex component

endoplasmic reticulum

P932

1635383

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