NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway

	NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway
	Shen, Jie 1,2,3; Yang, Zhongzheng 1,2,4; Wang, Jiaolong 1,2; Zhao, Bin 1,2; Lan, Wenxian 1,2; Wang, Chunxi 1,2; Zhang, Xu 5; Wild, Cody J.6,7; Liu, Maili 5; Xu, Zhaohui 6,7
刊名	SCIENTIFIC REPORTS
	2016-12-07
卷号	6
英文摘要	As an AAA-ATPase, Vps4 is important for function of multivesicular bodies (MVB) sorting pathway, which involves in cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. The activity of Vps4 is stimulated by the interactions between Vta1 N-terminus (named as Vta1NTD) and Did2 fragment (176-204 aa) (termed as Did2(176-204)) or Vps60 (128-186 aa) (termed as Vps60(128-186)). The structural basis of how Vta1NTD binds to Did2(176-204) is still unclear. To address this, in this report, the structure of Did2(176-204) in complex with Vta1NTD was determined by NMR techniques, demonstrating that Did2(176-204) interacts with Vta1NTD through its helix alpha 6' extending over the 2nd and the 3rd alpha-helices of Vta1NTD microtubule interacting and transport 1 (MIT1) domain. The residues within Did2(176-204) helix a6' in the interface make up of an amino acid sequence as E-192' xxL(195)' xxR(198)' L-199' xxL(202)' R-203', identical to type 1 MIT-interacting motif (MIM1) (D/E) xxLxxRLxxL(K/R) of CHMP1A(180-196) observed in Vps4-CHMP1A complex structure, indicating that Did2 binds to Vta1NTD through canonical MIM1 interactions. Moreover, the Did2 binding does not result in Vta1NTD significant conformational changes, revealing that Did2, similar to Vps60, enhances Vta1 stimulation of Vps4 ATPase activity in an indirect manner.
WOS标题词	Science & Technology
类目[WOS]	Multidisciplinary Sciences
研究领域[WOS]	Science & Technology - Other Topics
关键词[WOS]	ESCRT-III RECOGNITION ; AAA-ATPASE VPS4 ; STRUCTURAL BASIS ; MEMBRANE ASSOCIATION ; CHEMICAL-SHIFT ; BODY PATHWAY ; PROTEIN ; MACHINERY ; COMPLEXES ; CYTOKINESIS
收录类别	SCI
语种	英语
WOS记录号	WOS:000389750700001
内容类型	期刊论文
源URL	[http://124.16.173.210/handle/834782/2281]
专题	天津工业生物技术研究所_总体研究部_期刊论文
作者单位	1.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, 345 Lingling Rd, Shanghai 200032, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Organ Chem, Collaborat Innovat Ctr Chem Life Sci, 345 Lingling Rd, Shanghai 200032, Peoples R China 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin Airport Econ Area, 32 XiQiDao, Tianjin 300308, Peoples R China 4.Wuhan Inst Biotechnol, Publ Technol Serv Platform, 666 Gaoxin Rd, Wuhan 430075, Peoples R China 5.Chinese Acad Sci, Wuhan Inst Phys & Math, State Key Lab Magnet Resonance & Atom & Mol Phys, 30 West Xiaohongshan Rd, Wuhan 430071, Peoples R China 6.Univ Michigan, Sch Med, Life Sci Inst, 210 Washtenaw Ave, Ann Arbor, MI 48109 USA 7.Univ Michigan, Sch Med, Dept Biol Chem, 210 Washtenaw Ave, Ann Arbor, MI 48109 USA
推荐引用方式 GB/T 7714	Shen, Jie,Yang, Zhongzheng,Wang, Jiaolong,et al. NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway[J]. SCIENTIFIC REPORTS,2016,6.
APA	Shen, Jie.,Yang, Zhongzheng.,Wang, Jiaolong.,Zhao, Bin.,Lan, Wenxian.,...&Cao, Chunyang.(2016).NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway.SCIENTIFIC REPORTS,6.
MLA	Shen, Jie,et al."NMR studies on the interactions between yeast Vta1 and Did2 during the multivesicular bodies sorting pathway".SCIENTIFIC REPORTS 6(2016).