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....

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Bibliographic Details
Published in:EMBO reports 2002-10, Vol.3 (10), p.988-994
Main Authors: Choi, Jae H, Bertram, Paula G, Drenan, Ryan, Carvalho, John, Zhou, Heather H, Zheng, X F Steven
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Carrier Proteins
Cattle
Cell Line
HeLa Cells
Humans
Immunophilins - chemistry
Immunophilins - physiology
Microtubule-Associated Proteins - chemistry
Microtubule-Associated Proteins - metabolism
Models, Biological
Neoplasm Proteins
Phosphorylation
Phosphotransferases (Alcohol Group Acceptor)
Protein Binding
Protein Structure, Tertiary
Scientific Report
Sirolimus - pharmacology
Time Factors
TOR Serine-Threonine Kinases
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Summary: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.
ISSN:1469-221X
1469-3178
DOI:10.1093/embo-reports/kvf197