The role of SRC-CAS interactions in cellular transformation: ectopic expression of the carboxy terminus of CAS inhibits SRC-CAS interaction but has no effect on cellular transformation

M R Burnham, M T Harte, A H Bouton

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Several lines of evidence indicate that the adapter molecule p130CAS (crk-associated substrate (CAS)) is required for src-mediated cellular transformation. CAS has been shown to be heavily tyrosine-phosphorylated in src-transformed cells, and genetic variants of src that are deficient in CAS binding are also unable to mediate cellular transformation. In this report, we investigated whether CAS phosphorylation and/or its association with src are required elements of the transformation process. Expression of the carboxy-terminal src binding domain of CAS in Rat 1 fibroblasts expressing a temperature-sensitive allele of v-src inhibited the formation of src-CAS complexes and also inhibited tyrosine phosphorylation of CAS. However, expression of this protein had no effect on morphological transformation, src-mediated actin rearrangements, or anchorage-independent growth of these cells when grown at the src-permissive temperature. Thus, the ability of activated src to mediate cellular transformation is either largely independent of endogenous CAS phosphorylation and/or its association with CAS or, alternatively, the carboxy-terminus of CAS may substitute for endogenous CAS in the process of src-mediated transformation.
Original languageEnglish
Pages (from-to)20-31
Number of pages12
JournalMolecular Carcinogenesis
Volume26
Issue number1
Publication statusPublished - Sep 1999

Keywords

  • Actins
  • Animals
  • Cell Adhesion
  • Cell Transformation, Neoplastic
  • Oncogene Protein pp60(v-src)
  • Phosphorylation
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-cbl
  • Rats
  • Tyrosine
  • Ubiquitin-Protein Ligases
  • src-Family Kinases

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