Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties

Ippeita Dan, Shao En Ong, Norinobu M. Watanabe, Blagoy Blagoev, Mogens M. Nielsen, Eriko Kajikawa, Troels Z. Kristiansen, Matthias Mann, Akhilesh Pandey

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5929-5939
Number of pages11
JournalJournal of Biological Chemistry
Volume277
Issue number8
DOIs
StatePublished - Feb 22 2002
Externally publishedYes

Fingerprint

Cloning
Organism Cloning
Phosphotransferases
Apoptosis
Caspase 3
germinal center kinases
Cells
Two-Hybrid System Techniques
Myelin Basic Protein
Mitogen-Activated Protein Kinases
Hybrid systems
Yeast
Machinery

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties. / Dan, Ippeita; Ong, Shao En; Watanabe, Norinobu M.; Blagoev, Blagoy; Nielsen, Mogens M.; Kajikawa, Eriko; Kristiansen, Troels Z.; Mann, Matthias; Pandey, Akhilesh.

In: Journal of Biological Chemistry, Vol. 277, No. 8, 22.02.2002, p. 5929-5939.

Research output: Contribution to journalArticle

Dan, I, Ong, SE, Watanabe, NM, Blagoev, B, Nielsen, MM, Kajikawa, E, Kristiansen, TZ, Mann, M & Pandey, A 2002, 'Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties', Journal of Biological Chemistry, vol. 277, no. 8, pp. 5929-5939. https://doi.org/10.1074/jbc.M110882200
Dan, Ippeita ; Ong, Shao En ; Watanabe, Norinobu M. ; Blagoev, Blagoy ; Nielsen, Mogens M. ; Kajikawa, Eriko ; Kristiansen, Troels Z. ; Mann, Matthias ; Pandey, Akhilesh. / Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 8. pp. 5929-5939.
@article{9ff666427e4a4290957f7abd451a2920,
title = "Cloning of MASK, a novel member of the mammalian germinal center kinase III subfamily, with apoptosis-inducing properties",
abstract = "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.",
author = "Ippeita Dan and Ong, {Shao En} and Watanabe, {Norinobu M.} and Blagoy Blagoev and Nielsen, {Mogens M.} and Eriko Kajikawa and Kristiansen, {Troels Z.} and Matthias Mann and Akhilesh Pandey",
year = "2002",
month = "2",
day = "22",
doi = "10.1074/jbc.M110882200",
language = "English (US)",
volume = "277",
pages = "5929--5939",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "8",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0037155191&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037155191&partnerID=8YFLogxK

U2 - 10.1074/jbc.M110882200

DO - 10.1074/jbc.M110882200

M3 - Article

C2 - 11741893

AN - SCOPUS:0037155191

VL - 277

SP - 5929

EP - 5939

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 8

ER -