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Protein Kinase D Is A Positive Regulator Of Bit1 Apoptotic Function, Hector Biliran, Y. Jan, R. Chen, E. Ruoslahti
Protein Kinase D Is A Positive Regulator Of Bit1 Apoptotic Function, Hector Biliran, Y. Jan, R. Chen, E. Ruoslahti
Faculty and Staff Publications
Bit1 (Bcl-2 inhibitor of transcription) is a mitochondrial protein that induces caspase-independent apoptosis upon its release into the cytoplasm. Bit1 is primarily associated with anoikis (cell death induced by detachment from the extracellular matrix), because the apoptotic function of Bit1 is inhibited by integrin-mediated cell attachment but not by many other antiapoptotic treatments. Here, we show that protein kinase D (PKD) regulates Bit1 apoptotic function. Overexpression of constitutively active PKD or PKD activation by treatment with phorbol 12-myristate 13-acetate results in phosphorylation of two serine residues (Ser5 and Ser87) in a form of Bit1 that is confined to the cytoplasm …