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A Novel Mechanism of Regulating the ATPase VPS4 by Its Cofactor LIP5 and the Endosomal Sorting Complex Required for Transport (ESCRT)-III Protein CHMP5

Autor: Zhaohui Xu, Yuan Liu, Yan Li, Cody Vild, Emily Zhen Guo

Publikováno v: Journal of Biological Chemistry. 290:7291-7303

Disassembly of the endosomal sorting complex required for transport (ESCRT) machinery from biological membranes is a critical final step in cellular processes that require the ESCRT function. This reaction is catalyzed by VPS4, an AAA-ATPase whose ac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd4fd2c1f2a013337f882f6d8950843c
https://doi.org/10.1074/jbc.m114.616730

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1H, 13C and 15N resonance assignments of the N-terminal domain of Vta1–Vps60 peptide complex

Autor: Jie Shen, Maili Liu, Wenxian Lan, Zhaohui Xu, Cody Vild, Zhongzheng Yang, Xu Zhang, Chunyang Cao

Publikováno v: Biomolecular NMR Assignments. 7:331-334

Vta1 and Vps60 are two ESCRT associated proteins, their direct interaction enhances Vps4 ATPase activity. The N-terminal domain of Vta1 (residues 1–167aa, named as Vta1NTD) contains two tandem MIT domains, which specifically recognize Vps60 and Did

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::470011ea61c4d20d0197e09756cee1bd
https://doi.org/10.1007/s12104-012-9439-1

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Vfa1 binds to the N-terminal microtubule-interacting and trafficking (MIT) domain of Vps4 and stimulates its ATPase activity

Autor: Cody Vild, Zhaohui Xu

Publikováno v: The Journal of biological chemistry. 289(15)

The endosomal sorting complexes required for transport (ESCRT) are responsible for multivesicular body biogenesis, membrane abscission during cytokinesis, and retroviral budding. They function as transiently assembled molecular complexes on the membr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1c15472aed393be371f257ee5115482
https://pubmed.ncbi.nlm.nih.gov/24567329

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Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway

Autor: Jiaying Ju, Jianping Liu, Xu Zhang, Jie Shen, Zhongzheng Yang, Chunyang Cao, Cody Vild, Bin Zhao, Fuchun Gong, Maili Liu, Wenxian Lan, Zhaohui Xu

Publikováno v: The Journal of biological chemistry. 287(52)

The AAA-ATPase Vps4 is critical for function of the multivesicular body sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5821480e2cbc60fbbee246080470d39
https://pubmed.ncbi.nlm.nih.gov/23105107

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¹H, ¹³C and ¹⁵N resonance assignments of the N-terminal domain of Vta1-Vps60 peptide complex

Autor: Zhongzheng, Yang, Jie, Shen, Xu, Zhang, Cody, Vild, Wenxian, Lan, Maili, Liu, Zhaohui, Xu, Chunyang, Cao

Publikováno v: Biomolecular NMR assignments. 7(2)

Vta1 and Vps60 are two ESCRT associated proteins, their direct interaction enhances Vps4 ATPase activity. The N-terminal domain of Vta1 (residues 1-167aa, named as Vta1NTD) contains two tandem MIT domains, which specifically recognize Vps60 and Did2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ce8bd205331154a2f08d772fdfed24a7
https://pubmed.ncbi.nlm.nih.gov/23132527

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