Gene interactions and pathways from curated databases and text-mining
EMBO Rep 2002, PMID: 12231510

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

Choi, Jae H; Bertram, Paula G; Drenan, Ryan; Carvalho, John; Zhou, Heather H; Zheng, X F Steven

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.

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Text Mining Data

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Manually curated Databases

  • IRef Biogrid Interaction: CLIP1 — MTOR (direct interaction, pull down)
  • IRef Biogrid Interaction: CLIP1 — MTOR (physical association, affinity chromatography technology)
  • IRef Hprd Interaction: CLIP1 — MTOR (in vivo)
  • IRef Innatedb Interaction: CLIP1 — MTOR (unknown, -)
  • NCI Pathway Database mTOR signaling pathway: mTORC1 complex (MTOR-MLST8-RPTOR) → CLIP170 (CLIP1) (modification, activates)
    Evidence: mutant phenotype, assay, physical interaction
In total, 6 gene pairs are associated to this article in curated databases