The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A
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 mutantsAssembly, organization, and function of the COPII coatMultifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane TraffickingDeterminants of Glycosaminoglycan (GAG) StructureVesicle-mediated export from the ER: COPII coat function and regulationSmy2p 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) 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.Annexins as Overlooked Regulators of Membrane Trafficking in Plant CellsVesicular 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 calciumCK2 phosphorylates Sec31 and regulates ER-To-Golgi traffickingA 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 compartmentsNuclear 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
0c4aa9f7c7619e94e0a6d23190089a270f7ee03110583ce5d560d94c1c89c6f1c95125408bcafb4e2a3885e3dd19ab2836dad18328feef5238ef4bcc31c6b844b95b926cdb47e502a8decc9701e9aed44a614db57bf88f783e1dd248da39ba533ff5475b50c52b1f41e270c5a8d9b35fa106516cc93a631752242b04d7b12256d1db2186745b597d0c00d5af55d4fed7be7f3939d236b0785664bce20110a269d285d4c4f2a7679f62090f918732aad261c40fe8
P248
Q24294782-E083D224-E3FA-4CA2-8024-3B4F82C40C49Q24311319-A7B315C5-C9F3-4972-9539-22D32135DBD3Q24655263-0F4FE787-7EEC-40F2-85DA-8A882C89D7C2Q26738429-672EB684-6AD6-4B81-96F1-DD4CEFBC1198Q26797302-28C0EE4F-C4A6-4D5E-9E5A-8AFA1EF85AD4Q26821930-A6A40E30-C55A-4B58-89E1-0D2EA606C511Q27933025-34C06780-7982-4912-8964-D8C8C3884D18Q27933669-B1C4B73A-F778-4F77-A408-E49F34C98675Q27938069-404AC0AB-B6BB-429B-8995-2192916013EAQ28975756-6A532939-8760-4E79-A68B-ED5BA4CC9D24Q28975761-2D051763-0593-49A8-8181-2AA8C8BA660CQ28975786-C72CFAE3-B84E-4ADA-8D92-E6AEF774C2B2Q31140170-917BD493-4E42-4D4E-8EDC-0CEE0CD9326EQ33624905-A8650B90-3B20-4675-AD71-F30142BA43C3Q33721151-9BE58342-FB75-4165-95B6-F0DB2540166DQ33974677-AFB8BE7F-9B3E-4022-86D7-AD52CD644F46Q34141117-ECC54380-7B0F-4807-829C-C100120EDE44Q34563010-AAFC424C-3C43-40F7-9F66-49B6398434ECQ35103974-FC5F2B81-FCC3-4B38-A7B5-1FC1CA4A91E2Q35658408-F1A7F98A-EB15-4047-A77D-8FCA213FC50EQ36044989-712A116C-22F8-4AE3-A373-47316EAB18CCQ37479337-94DF771F-A51B-41B2-9AB0-9140B5980926Q37619765-B052D449-5B81-4DD2-A3AD-F6C7035C6B21Q37709368-03FC237F-DA00-41E9-AF51-1DC24AEC9B71Q37807408-DD382E31-BF65-411A-A9DB-90B856D66C3EQ37904897-A5174963-E1B4-4AC8-BEF9-354979675BA8Q37970881-EFFEED35-CAC5-46FC-85A9-5029B5F8592FQ38267212-8BE744D6-6832-4C7A-810D-988FE88EE9A2Q38529922-95FAAAE0-6953-479B-B413-786CF1808730Q39076020-F957257F-83E8-48DF-8401-37A11CB08CC5Q41251534-52A4D11D-2157-4DF6-8B3F-56F3039C0EB3Q41881232-88096DBB-CD05-483E-B363-64733DB555BCQ42135943-382239F3-9008-4248-90FC-E835DFFFE269Q42237955-116F7C3C-E7A6-4C9A-ACD5-D3BFC0CC47F7Q42319786-7B261F8D-F5D5-40FF-AD1F-D2E7DE457283Q43159984-44F883DD-A428-4723-BED2-3BF73B16B48DQ47867485-FB435488-220F-4EFB-8DCF-39FB0C32DB48Q48133011-2C1CFC37-C06B-4F81-AC15-035AA12C2698Q50541417-45688F63-30CB-4B90-89B9-04619707350CQ55262182-1A5C16E0-006A-4C78-91D8-C45DF653269D
P2860
The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A
description
2006 nî lūn-bûn
@nan
2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@ast
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en-gb
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@nl
type
label
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@ast
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en-gb
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@nl
prefLabel
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@ast
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en-gb
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@nl
P2093
P2860
P921
P3181
P356
P1476
The Ca2+-binding protein ALG-2 ...... zes the localization of Sec31A
@en
P2093
Akinori Yamasaki
Akitsugu Yamamoto
Katsuko Tani
Masayuki Komada
Naomi Kitamura
P2860
P304
P3181
P356
10.1091/MBC.E06-05-0444
P407
P577
2006-11-01T00:00:00Z