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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.

Pubmed ID: 12231510


  • Choi JH
  • Bertram PG
  • Drenan R
  • Carvalho J
  • Zhou HH
  • Zheng XF


EMBO reports

Publication Data

October 8, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: R01CA77668
  • Agency: NIGMS NIH HHS, Id: R01GM62817

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
  • TOR Serine-Threonine Kinases
  • Time Factors