The tumour suppressor RASSF1A is a novel substrate of PKC

Sunil K. Verma, Trivadi S. Ganesan, Peter J. Parker

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Ras association domain family 1A (RASSF1A) is a tumour suppressor that contains an amino-terminal cysteine-rich region, similar to the diacylglycerol (DAG)-binding domain (C1 domain) found in the protein kinase C (PKC) family of proteins, and a carboxy-terminal Ras-association (RA) domain. In the present study, RASSF1A was identified as a substrate for PKC. Using classical biochemical approaches, it was established that S197 and S203 within the RA domain of RASSF1A are phosphorylated by PKC in vitro and in vivo. Unlike the WT protein, the S197, 203D double mutant of RASSF1A failed to modulate microtubule organization and perinuclear vimentin collapse. By contrast, the equivalent AA mutant of RASSF1A phenocopied the WT protein. These findings indicate that PKC phosphorylation of RASSF1A regulates its ability to reorganize the microtubule network.

Original languageEnglish (US)
Pages (from-to)2270-2276
Number of pages7
JournalFEBS Letters
Volume582
Issue number15
DOIs
StatePublished - Jun 25 2008

Keywords

  • Microtubule organization
  • Protein kinase C
  • RASSF1A
  • Vimentin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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