Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae.
Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae.
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Pep3p/Pep5p 复合物:囊泡运输到酿酒酵母液泡的多个步骤中的假定对接因子。
DOI:
10.1093/genetics/156.1.105
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发表时间:
2000
期刊:
影响因子:
3.3
通讯作者:
Jones,EW
中科院分区:
文献类型:
--
作者:
Srivastava,A;Woolford,CA;Jones,EW
Pep3p and Pep5p are known to be necessary for trafficking of hydrolase precursors to the vacuole and for vacuolar biogenesis. These proteins are present in a hetero-oligomeric complex that mediates transport at the vacuolar membrane.PEP5interacts genetically withVPS8, implicating Pep5p in the earlier Golgi to endosome step and/or in recycling from the endosome to the Golgi. To understand further the cellular roles of Pep3p and Pep5p, we isolated and characterized a set ofpep3conditional mutants. Characterization of mutants revealed thatpep3tsmutants are defective in the endosomal and nonendosomal Golgi to vacuole transport pathways, in the cytoplasm to vacuole targeting pathway, in recycling from the endosome back to the late Golgi, and in endocytosis.PEP3interacts genetically with two members of the endosomal SNARE complex,PEP12(t-SNARE) andPEP7(homologue of mammalian EEA1); Pep3p and Pep5p associate physically with Pep7p as revealed by two-hybrid analysis. Our results suggest that a core Pep3p/Pep5p complex promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole. We propose that this complex may be responsible for tethering transport vesicles on target membranes.
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影响因子:
3.3
作者:
Webb,GC;Zhang,J;Garlow,SJ;Wesp,A;Riezman,H;Jones,EW
通讯作者:
Jones,EW
影响因子:
3.3
作者:
P. James;J. Halladay;E. Craig
通讯作者:
P. James;J. Halladay;E. Craig
影响因子:
3.3
作者:
E. W. Jones
通讯作者:
E. W. Jones
影响因子:
16
作者:
Sevrioukov, EA;He, JP;Krämer, H
通讯作者:
Krämer, H