Identification of Rictor as a Novel Substrate of Polo-like kinase

Tian Shao, Xiaoqi Liu

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Plk1 has been essentially described as a critical regulator of many mitotic events. However, increasing evidence supports the notion that its molecular functions are not restricted to the cell cycle. In particular, recent reports suggest the existence of a molecular and functional link between Plk1 and the mammalian target of rapamycin (mTOR) pathway, which controls cell growth and proliferation via the raptor-mTOR (TORC1) and rictor-mTOR (TORC2) protein complexes. Herein, we have identified rapamycin-insensitive companion of mTOR (Rictor), a core component of mTORC2, as a new Plk1 substrate and have shown that Plk1 phosphorylates Rictor at Ser1162 in vitro and in vivo. Surprisingly, cells expressing the unphosphorylatable mutant (S1162A) of Rictor did not show any effect on well characterized canonical PI3K-mTOR pathway. However, we found that cells expressing the unphosphorylatable form of Rictor have an elevated level of mSin1 isoform (mSin1.5). Considering that mSin1.5-containing mTORC2 was reported to associate with stress signaling, we propose that phosphorylation of Rictor at Ser1162 by Plk1 might be involved in a novel signaling pathway by regulating the mSin1.5-defined mTORC2.

Original languageEnglish
Pages (from-to)755-760
Number of pages6
JournalCell Cycle
Volume14
Issue number5
DOIs
StatePublished - Mar 13 2015

Bibliographical note

Funding Information:
This work was supported by NIH grant R01CA157429 (X. L.), NSF grant MCB-1049693 (X.L.), ACS grant RSG-13–073 (X.L.), and NIH grant P30 CA023168 for Purdue Center for Cancer Research.

Publisher Copyright:
© 2015 Taylor & Francis Group, LLC.

Keywords

  • Cell cycle
  • MSin1
  • MTORC
  • Phosphorylation
  • Plk1
  • Rictor

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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