The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase.

Autor: Choi, Jae H., Bertram, Paula G., Drenan, Ryan, Carvalho, John, Zhou, Heather H., Zheng, X. F. Steven
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Zdroj: EMBO Reports; Oct2002, Vol. 3 Issue 10, p988-994, 7p
Abstrakt: CLIP-170/Restin belongs to a family of conserved microtubule (MT)-associated proteins, which are important for MT organization and functions. CLIP-170 is a phosphoprotein and phosphorylation is thought to regulate the binding of CLIP-170 to MTs. However, little is known about the kinase(s) involved. In this study, we show that FKBP12-rapamycin-associated protein (FRAP, also called mTOR/RAFT) interacts with CLIP-170. CLIP-170 is phosphorylated in vivo at multiple sites, including rapamycin-sensitive and -insensitive sites, and is phosphorylated by FRAP in vitro at the rapamycin-sensitive sites. In addition, rapamycin inhibited the ability of CLIP-170 to bind to MTs. Our observations suggest that multiple CLIP-170 kinases are involved in positive and negative control of CLIP-170, and FRAP is a CLIP-170 kinase positively regulating the MT-binding behavior of CLIP-170. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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