小GTP结合蛋白Sar1p依赖于Sec12p的膜结合促进内质网形成运输小泡。
Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p promotes formation of transport vesicles from the ER.
作者信息
d'Enfert C, Wuestehube L J, Lila T, Schekman R
机构信息
Division of Biochemistry and Molecular Biology, University of California, Berkeley 94720.
出版信息
J Cell Biol. 1991 Aug;114(4):663-70. doi: 10.1083/jcb.114.4.663.
Abstract
Sec12p is an integral membrane protein required in vivo and in vitro for the formation of transport vesicles generated from the ER. Vesicle budding and protein transport from ER membranes containing normal levels of Sec12p is inhibited in vitro by addition of microsomes isolated from a Sec12p-overproducing strain. Inhibition is attributable to titration of a limiting cytosolic protein. This limitation is overcome by addition of a highly enriched fraction of soluble Sar1p, a small GTP-binding protein, shown previously to be essential for protein transport from the ER and whose gene has been shown to interact genetically with sec12. Furthermore, Sar1p binding to isolated membranes is enhanced at elevated levels of Sec12p. Sar1p-Sec12p interaction may regulate the initiation of vesicle budding from the ER.
摘要
Sec12p是一种整合膜蛋白，在体内和体外对于内质网产生的运输小泡的形成都是必需的。从过量表达Sec12p的菌株中分离出的微粒体加入体外反应体系后，含有正常水平Sec12p的内质网膜的小泡出芽和蛋白质运输受到抑制。这种抑制归因于一种有限的胞质蛋白的滴定。通过添加高度富集的可溶性Sar1p组分可以克服这种限制，Sar1p是一种小GTP结合蛋白，先前已证明其对于从内质网的蛋白质运输至关重要，并且其基因已证明与sec12存在遗传相互作用。此外，在Sec12p水平升高时，Sar1p与分离膜的结合增强。Sar1p-Sec12p相互作用可能调节内质网小泡出芽的起始。
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