The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase.
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.
Mesh Terms:
Animals, Binding Sites, Carrier Proteins, Cattle, Cell Line, Hela Cells, Humans, Immunophilins, Microtubule-Associated Proteins, Models, Biological, Neoplasm Proteins, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor), Protein Binding, Protein Structure, Tertiary, Sirolimus, Time Factors
Animals, Binding Sites, Carrier Proteins, Cattle, Cell Line, Hela Cells, Humans, Immunophilins, Microtubule-Associated Proteins, Models, Biological, Neoplasm Proteins, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor), Protein Binding, Protein Structure, Tertiary, Sirolimus, Time Factors
EMBO Rep.
Date: Oct. 01, 2002
PubMed ID: 12231510
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