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    Caspase-mediated cleavage and functional changes of hematopoietic progenitor kinase 1 (HPK1)

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    Authors
    Chen, Yi-Rong
    Meyer, Christian F
    Ahmed, Bushra Y.
    Yao, Zhengbin
    Tan, Tse-Hua
    Issue Date
    1999
    
    Metadata
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    Abstract
    Activation of c-Jun N-terminal kinase (JNK) by Fas ligation is caspase-dependent, suggesting that caspases may regulate activators of the JNK pathway. Here, we report that an upstream activator of JNK, hematopoietic progenitor kinase 1 (HPK1), was cleaved during apoptosis. Cleavage of HPK1 was blocked by peptide inhibitors for caspases. HPK1 was efficiently processed by recombinant caspase 3 in vitro. A conserved caspase recognition site, DDVD (amino acids 382 - 385), was found in the HPK1 protein sequence. By testing HPK1 proteins with in vivo and in vitro cleavage assays, we showed that aspartic acid residue 385 is the target for caspases. HPK1 cleavage separated the amino N-terminal kinase domain from the carboxyl C-terminal regulatory domain, and enhanced HPK1 kinase activity. Unlike the full-length HPK1, the N-terminal cleaved product failed to bind adaptor molecules Grb2 (growth factor receptor-bound protein 2) and Crk (CT10 regulator of kinase). The C-terminal fragment, although having three proline-rich domains, bound to Grb2 and Crk less efficiently than the full-length HPK1 protein. Taken together, the cleavage of HPK1 by caspase profoundly changed its biochemical properties.
    Citation
    Chen Y-R., Meyer C., Ahmed B. Y., Yao Z. and Tan T-H. (1999) 'Caspase-mediated cleavage and functional changes of hematopoietic progenitor kinase 1 (HPK1' Oncogene, 18(51),pp.7370-7377
    Publisher
    Nature Publishing Group
    Journal
    Oncogene
    URI
    http://hdl.handle.net/10547/302092
    DOI
    10.1038/sj.onc.1203116
    Additional Links
    http://www.nature.com/doifinder/10.1038/sj.onc.1203116
    Type
    Article
    Language
    en
    ISSN
    0950-9232
    ae974a485f413a2113503eed53cd6c53
    10.1038/sj.onc.1203116
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

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