期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 275, 期 2, 页码 261-267出版社
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2000.3295
关键词
ADAM 12; disintegrin; metalloprotease; trafficking; trans-Golgi network
We have investigated the trafficking of the membrane-anchored form of human ADAM 12 (ADAM 12-L) fused to a green fluorescence protein tag. Subcellular localization of the protein in transiently transfected cells was determined by fluorescence microscopy and trypsin sensitivity. Full-length ADAM 12-L was retained in a perinuclear compartment, which was shown to be the trans-Glolgi network. In contrast, ADAM 12-L lacking the cytoplasmic domain reached the cell surface. Based on analysis of deletions and mutations of the cytoplasmic tail of ADAM 12-L, the retention signal is comprised of both the cytoplasmic and transmembrane domains, but not the Src homology 3 domain (SH3) binding sites. These results raise the possibility that a trafficking checkpoint in the trans-Gola network is one of the cellular mechanisms for regulation of ADAM 12-L function, by allowing a rapid release of ADAM 12-L to the cell surface under specific stimuli. (C) 2000 Academic Press.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据