Shoukat Dedhar, University of British Columbia
Biochemistry and Molecular Biology
Professor
Vancouver, British Columbia
sdedhar@interchange.ubc.ca
Office:
(604) 875-5655
Expert In
Bio/Research
Dr. Dedhar’s laboratory is investigating the interaction of the integrin subunits with intracellular proteins and the mechanism of signal transduction mediated by these receptors. Members of the laboratory have recently obtained evidence for the interaction of a 60 kilodalton calcium binding prot...
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Bio/Research
Dr. Dedhar’s laboratory is investigating the interaction of the integrin subunits with intracellular proteins and the mechanism of signal transduction mediated by these receptors. Members of the laboratory have recently obtained evidence for the interaction of a 60 kilodalton calcium binding protein with a highly conserved amino acid sequence found in the cytoplasmic domain of all integrin alpha subunits.
This protein, also called calreticulin, is essential for integrin function since integrins in calreticulin ”knock out” cells fail to interact with their ligands. Calreticulin may also be involved in transducing signals to the nucleus where it may influence gene expression by binding to nuclear transcription factors such as steroid receptors. Evidence has also been obtained in the laboratory for the interaction of a novel serine/threonine protein kinase (ILK) with the cytoplasmic domain of the integrin beta1 subunit. Overexpression of this kinase in epithelial cells induced anchorage-independent growth and tumorigenicity. ILK regulates adhesion dependent cell cycle progression as well as epithelial-mesenchymal transformation. Elevated expression of, or mutations in, this kinase may be crucial in transformation.
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This protein, also called calreticulin, is essential for integrin function since integrins in calreticulin ”knock out” cells fail to interact with their ligands. Calreticulin may also be involved in transducing signals to the nucleus where it may influence gene expression by binding to nuclear transcription factors such as steroid receptors. Evidence has also been obtained in the laboratory for the interaction of a novel serine/threonine protein kinase (ILK) with the cytoplasmic domain of the integrin beta1 subunit. Overexpression of this kinase in epithelial cells induced anchorage-independent growth and tumorigenicity. ILK regulates adhesion dependent cell cycle progression as well as epithelial-mesenchymal transformation. Elevated expression of, or mutations in, this kinase may be crucial in transformation.
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