Organization of functional domains in the docking protein p130Cas

Fariborz Nasertorabi, Miguel Garcia-Guzman, Klára Briknarová, Elise Larsen, Marnie L. Havert, Kristiina Vuori, Kathryn R. Ely

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


The docking protein p130Cas becomes phosphorylated upon cell adhesion to extracellular matrix proteins, and is thought to play an essential role in cell transformation. Cas transmits signals through interactions with the Src-homology 3 (SH3) and Src-homology 2 domains of FAK or v-Crk signaling molecules, or with 14-3-3 protein, as well as phosphatases PTP1B and PTP-PEST. The large (130 kDa), multi-domain Cas molecule contains an SH3 domain, a Src-binding domain, a serine-rich protein interaction region, and a C-terminal region that participates in protein interactions implicated in antiestrogen resistance in breast cancer. In this study, as part of a long-term goal to examine the protein interactions of Cas by X-ray crystallography and nuclear magnetic resonance spectroscopy, molecular constructs were designed to express two adjacent domains, the serine-rich domain and the Src-binding domain, that each participate in intermolecular contacts dependent on protein phosphorylation. The protein products are soluble, homogeneous, monodisperse, and highly suitable for structural studies to define the role of Cas in integrin-mediated cell signaling.

Original languageEnglish
Pages (from-to)993-998
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Nov 19 2004


  • 14-3-3 protein
  • Cas family proteins
  • Integrin signaling
  • Protein design
  • Protein phosphorylation
  • Src family kinases


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