TY - JOUR
T1 - Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties
AU - Dan, Ippeita
AU - Ong, Shao En
AU - Watanabe, Norinobu M.
AU - Blagoev, Blagoy
AU - Nielsen, Mogens M.
AU - Kajikawa, Eriko
AU - Kristiansen, Troels Z.
AU - Mann, Matthias
AU - Pandey, Akhilesh
PY - 2002/2/22
Y1 - 2002/2/22
N2 - We have cloned a novel human GCK family kinase that has been designated as MASK (Mst3 and SOK1-related kinase). MASK is widely expressed and encodes a protein of 416 amino acid residues, with an N-terminal kinase domain and a unique C-terminal region. Like other GCK-III subfamily kinases, MASK not activate any mitogen-activated protein kinase pathways. Wild type MASK, but not a form lacking the C terminus, exhibits homophilic binding in the yeast two-hybrid system and in coimmunoprecipitation experiments. Additionally, deletion of this C-terminal region of MASK leads to an increased kinase activity toward itself as well as toward an exogenous substrate, myelin basic protein. A potential caspase 3 cleavage site (DESDS) is present in the C-terminal region of MASK, and we show that MASK is cleaved in vitro by caspase 3. Finally, wild type and C-terminally truncated forms of MASK can both induce apoptosis upon overexpression in mammalian cells that is abrogated by CrmA, suggesting involvement of MASK in the apoptotic machinery in mammalian cells.
AB - We have cloned a novel human GCK family kinase that has been designated as MASK (Mst3 and SOK1-related kinase). MASK is widely expressed and encodes a protein of 416 amino acid residues, with an N-terminal kinase domain and a unique C-terminal region. Like other GCK-III subfamily kinases, MASK not activate any mitogen-activated protein kinase pathways. Wild type MASK, but not a form lacking the C terminus, exhibits homophilic binding in the yeast two-hybrid system and in coimmunoprecipitation experiments. Additionally, deletion of this C-terminal region of MASK leads to an increased kinase activity toward itself as well as toward an exogenous substrate, myelin basic protein. A potential caspase 3 cleavage site (DESDS) is present in the C-terminal region of MASK, and we show that MASK is cleaved in vitro by caspase 3. Finally, wild type and C-terminally truncated forms of MASK can both induce apoptosis upon overexpression in mammalian cells that is abrogated by CrmA, suggesting involvement of MASK in the apoptotic machinery in mammalian cells.
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U2 - 10.1074/jbc.M110882200
DO - 10.1074/jbc.M110882200
M3 - Article
C2 - 11741893
AN - SCOPUS:0037155191
SN - 0021-9258
VL - 277
SP - 5929
EP - 5939
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 8
ER -