期刊
JOURNAL OF CELL BIOLOGY
卷 181, 期 7, 页码 1073-1081出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200704079
关键词
-
类别
资金
- NIAID NIH HHS [K08AI062978, K08 AI062978] Funding Source: Medline
- NIDCR NIH HHS [1R03DE018425-01, R03 DE018425] Funding Source: Medline
- NIGMS NIH HHS [GM 0535393T] Funding Source: Medline
Signaling mucins are cell adhesion molecules that activate RAS/RHO guanosine triphosphatases and their effector mitogen-activated protein kinase (MAPK) pathways. We found that the Saccharomyces cerevisiae mucin Msb2p, which functions at the head of the Cdc42p-dependent MAPK pathway that controls filamentous growth, is processed into secreted and cell-associated forms. Cleavage of the extracellular inhibitory domain of Msb2p by the aspartyl protease Yps1p generated the active form of the protein by a mechanism incorporating cellular nutritional status. Activated Msb2p functioned through the tetraspan protein Sho1p to induce MAPK activation as well as cell polarization, which involved the Cdc42p guanine nucleotide exchange factor Cdc24p. We postulate that cleavage-dependent activation is a general feature of signaling mucins, which brings to light a novel regulatory aspect of this class of signaling adhesion molecule.
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