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酵母液泡的对接由类Ras GTP酶Ypt7p催化，此前Sec18p（NSF）进行了对称引发。

Docking of yeast vacuoles is catalyzed by the Ras-like GTPase Ypt7p after symmetric priming by Sec18p (NSF).

作者信息

Mayer A, Wickner W

机构信息

Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844, USA.

出版信息

J Cell Biol. 1997 Jan 27;136(2):307-17. doi: 10.1083/jcb.136.2.307.

DOI:10.1083/jcb.136.2.307
PMID:9015302
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2134819/
Abstract

Vacuole inheritance in yeast involves the formation of tubular and vesicular "segregation structures" which migrate into the bud and fuse there to establish the daughter cell vacuole. Vacuole fusion has been reconstituted in vitro and may be used as a model for an NSF-dependent reaction of priming, docking, and fusion. We have developed biochemical and microscopic assays for the docking step of in vitro vacuole fusion and characterized its requirements. The vacuoles must be primed for docking by the action of Sec17p (alpha-SNAP) and Sec18p (NSF). Priming is necessary for both fusion partners. It produces a labile state which requires rapid docking in order to lead productively to fusion. In addition to Sec17p/Sec18p, docking requires the activity of the Ras-like GTPase Ypt7p. Unlike Sec17p/Sec18p, which must act before docking, Ypt7p is directly involved in the docking process itself.

摘要

酵母中的液泡遗传涉及管状和囊泡状“分离结构”的形成，这些结构迁移到芽中并在那里融合，以建立子细胞液泡。液泡融合已在体外重建，可作为依赖 NSF 的引发、对接和融合反应的模型。我们已经开发了用于体外液泡融合对接步骤的生化和显微镜检测方法，并对其要求进行了表征。液泡必须通过 Sec17p（α-SNAP）和 Sec18p（NSF）的作用进行对接引发。引发对于两个融合伙伴都是必需的。它产生一种不稳定状态，需要快速对接才能有效地导致融合。除了 Sec17p/Sec18p 外，对接还需要类 Ras GTP 酶 Ypt7p 的活性。与必须在对接前起作用的 Sec17p/Sec18p 不同，Ypt7p 直接参与对接过程本身。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/99bbe2824d5f/JCB.mayer7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/c9958041aea6/JCB.mayer1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/3af90bd63bfc/JCB.mayer2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/8a0cc5a95826/JCB.mayer3a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/80d593b7ce9b/JCB.mayer4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/d9b1890c14b0/JCB.mayer6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/fe4d4511e1cf/JCB.mayer5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/99bbe2824d5f/JCB.mayer7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/c9958041aea6/JCB.mayer1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/3af90bd63bfc/JCB.mayer2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/8a0cc5a95826/JCB.mayer3a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/80d593b7ce9b/JCB.mayer4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/d9b1890c14b0/JCB.mayer6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/fe4d4511e1cf/JCB.mayer5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6e57/2134819/99bbe2824d5f/JCB.mayer7.jpg

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本文引用的文献

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J Cell Biol. 1997 Jan 27;136(2):299-306. doi: 10.1083/jcb.136.2.299.
2
Transport vesicle docking: SNAREs and associates.转运囊泡对接：可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体及其相关蛋白
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