Tip20p reaches out to Dsl1p to tether membranes

被引：6

作者：

Munson, Mary ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Mol Pharmacol & Biochem, Worcester, MA 01605 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2009年 / 16卷 / 02期

关键词：

COMPLEX; PROTEIN; VESICLE; ARCHITECTURE;

D O I：

10.1038/nsmb0209-100

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Large, multisubunit complexes have been implicated in tethering transport vesicles to organelle membranes before membrane fusion. New structures add to the growing list of tethering complexes that contain conserved helical bundle structures and provide a first glimpse of how these complexes are assembled.

引用

页码：100 / 102

页数：3

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[1] Tip20p reaches out to Dsl1p to tether membranes
Mary Munson
[J]. Nature Structural & Molecular Biology, 2009, 16 : 100 - 102
[2] Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
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Ren, Yi
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Hughson, Frederick M.
[J]. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2009, 16 (02) : 114 - 123
[3] Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
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Yi Ren
Philip D Jeffrey
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[J]. Nature Structural & Molecular Biology, 2009, 16 : 114 - 123
[4] Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
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[5] Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast (vol 16, pg 3963, 2005)
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[9] Tip20p prohibits back-fusion of COPII vesicles with the endoplasmic reticulum
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[J]. SCIENCE, 2004, 304 (5668) : 286 - 289
[10] Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules
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