Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3

Te Jung Lu; Chi Ying F. Huang; Chiun Jye Yuan; Yuan Chii Lee; Tzeng Horng Leu; Wen Chang Chang; Te Ling Lu; Wen Yih Jeng; Ming Derg Lai

doi:10.1016/j.jinorgbio.2005.03.003

Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3

Te Jung Lu, Chi Ying F. Huang, Chiun Jye Yuan, Yuan Chii Lee, Tzeng Horng Leu, Wen Chang Chang, Te Ling Lu, Wen Yih Jeng, Ming Derg Lai

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg⁺², Mn⁺², Zn²⁺, and Co²⁺) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe⁺² and Ca⁺² do not function as MST3 cofactors. Mn²⁺, Co ²⁺, and Mg²⁺-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn²⁺-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn²⁺ as the metal ion cofactor of a recombinant serine/threonine kinase.

Original language	English
Pages (from-to)	1306-1313
Number of pages	8
Journal	Journal of Inorganic Biochemistry
Volume	99
Issue number	6
DOIs	https://doi.org/10.1016/j.jinorgbio.2005.03.003
Publication status	Published - Jun 2005

Keywords

Autophosphorylation
Cobalt
Cofactor
Kinase
MST3
Zinc

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

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10.1016/j.jinorgbio.2005.03.003

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title = "Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3",

abstract = "We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg+2, Mn+2, Zn2+, and Co2+) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe+2 and Ca+2 do not function as MST3 cofactors. Mn2+, Co 2+, and Mg2+-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn2+-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn2+ as the metal ion cofactor of a recombinant serine/threonine kinase.",

keywords = "Autophosphorylation, Cobalt, Cofactor, Kinase, MST3, Zinc",

author = "Lu, {Te Jung} and Huang, {Chi Ying F.} and Yuan, {Chiun Jye} and Lee, {Yuan Chii} and Leu, {Tzeng Horng} and Chang, {Wen Chang} and Lu, {Te Ling} and Jeng, {Wen Yih} and Lai, {Ming Derg}",

note = "Funding Information: This work is in part supported by the Grant NSC93-2311-B-006-007 to Dr. Ming-Derg Lai from National Science Council, Taiwan, Republic of China, and in part by the program for promoting university academic excellence projects P1-FA-OP-1-4 to Dr. Wen-Chang Chang. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2005",

month = jun,

doi = "10.1016/j.jinorgbio.2005.03.003",

language = "English",

volume = "99",

pages = "1306--1313",

journal = "Journal of Inorganic Biochemistry",

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publisher = "Elsevier Inc.",

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T1 - Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3

AU - Lu, Te Jung

AU - Huang, Chi Ying F.

AU - Yuan, Chiun Jye

AU - Lee, Yuan Chii

AU - Leu, Tzeng Horng

AU - Chang, Wen Chang

AU - Lu, Te Ling

AU - Jeng, Wen Yih

AU - Lai, Ming Derg

N1 - Funding Information: This work is in part supported by the Grant NSC93-2311-B-006-007 to Dr. Ming-Derg Lai from National Science Council, Taiwan, Republic of China, and in part by the program for promoting university academic excellence projects P1-FA-OP-1-4 to Dr. Wen-Chang Chang. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2005/6

Y1 - 2005/6

N2 - We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg+2, Mn+2, Zn2+, and Co2+) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe+2 and Ca+2 do not function as MST3 cofactors. Mn2+, Co 2+, and Mg2+-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn2+-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn2+ as the metal ion cofactor of a recombinant serine/threonine kinase.

AB - We examined the metal ion cofactor preference for MST3 (mammalian Ste20-like kinase 3) of the Ste20 serine/threonine kinase family. Four metal ions (Mg+2, Mn+2, Zn2+, and Co2+) activate endogenous, exogenous, and baculovirus-expressed recombinant MST3 within the physiological concentration range. In contrast, Fe+2 and Ca+2 do not function as MST3 cofactors. Mn2+, Co 2+, and Mg2+-dependent autophosphorylation of MST3 is mainly on threonine residue while Zn2+-stimulated MST3 autophosphorylation is on both serine and threonine residues. The distinct autophosphorylation pattern on MST3 suggests that MST3 may exert various types of kinase reactions depending on the type of metal ion cofactor used. To our knowledge, this is the first report showing Zn2+ as the metal ion cofactor of a recombinant serine/threonine kinase.

KW - Autophosphorylation

KW - Cobalt

KW - Cofactor

KW - Kinase

KW - MST3

KW - Zinc

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Zinc ion acts as a cofactor for serine/threonine kinase MST3 and has a distinct role in autophosphorylation of MST3

Abstract

Keywords

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