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An update on transport vesicle tethering
被引:31
作者:
Brown, Frank C.
[1
]
Pfeffer, Suzanne R.
[1
]
机构:
[1] Stanford Univ, Dept Biochem, Sch Med, Stanford, CA 94305 USA
基金:
美国国家卫生研究院;
关键词:
Membrane traffic;
vesicle tethering;
Rab GTPase;
Golgi complex;
endosomes;
ENDOPLASMIC RETICULUM RETRIEVAL;
DEPENDENT MEMBRANE-FUSION;
RAB5 EFFECTOR EEA1;
SNARE COMPLEX;
NUCLEOTIDE EXCHANGE;
BINDING-SITES;
CIS-GOLGI;
COMPONENT;
PROTEIN;
DSL1P;
D O I:
10.3109/09687688.2010.501765
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:
Membrane trafficking involves the collection of cargo into nascent transport vesicles that bud off from a donor compartment, translocate along cytoskeletal tracks, and then dock and fuse with their target membranes. Docking and fusion involve initial interaction at a distance (tethering), followed by a closer interaction that leads to pairing of vesicle SNARE proteins (v-SNAREs) with target membrane SNAREs (t-SNAREs), thereby catalyzing vesicle fusion. When tethering cannot take place, transport vesicles accumulate in the cytoplasm. Tethering is generally carried out by two broad classes of molecules: extended, coiled-coil proteins such as the so-called Golgin proteins, or multi-subunit complexes such as the Exocyst, COG or Dsl complexes. This review will focus on the most recent advances in terms of our understanding of the mechanism by which tethers carry out their roles, and new structural insights into tethering complex transactions.
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页码:457 / 461
页数:5
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