Pervanadate induces Mammalian Ste20 Kinase 3 (MST3) tyrosine phosphorylation but not activation

Wei Chih Kan, Te Ling Lu, Pin Ling, Te Hsiu Lee, Chien Yu Cho, Chi Ying F. Huang, Wen-Yih Jeng, Yui Ping Weng, Chun Yen Chiang, Jin Bin Wu, Te Jung Lu

Research output: Contribution to journalArticle

Abstract

The yeast Ste20 (sterile) protein kinase, which is a serine/threonine kinase, responds to the stimulation of the G proteincoupled receptor (GPCR) pheromone receptor. Ste20 protein kinase serves as the critical component that links signaling from the GPCR/G proteins to the mitogen-activated protein kinase (MAPK) cascade in yeast. The yeast Ste20p functions as a MAP kinase kinase kinase kinase (MAP4K) in the pheromone response. Ste20-like kinases are structurally conserved from yeast to mammals. The mechanism by which MAP4K links GPCR to the MAPK pathway is less clearly defined in vertebrates. In addition to MAP4K, the tyrosine kinase cascade bridges G proteins and the MAPK pathway in vertebrate cells. Mammalian Ste20 Kinase 3 (MST3) has been categorized into the Ste20 family and has been reported to function in the regulation of cell polarity and migration. However, whether MST3 tyrosine phosphorylation regulates diverse signaling pathways is unknown. In this study, the tyrosine phosphatase inhibitor pervanadate was found to induce MST3 tyrosine phosphorylation in intact cells, and the activity of tyrosine-phosphorylated MST3 was measured. This tyrosine-directed phosphorylation was independent of MST3 activity. Parameters including protein conformation, Triton concentration and ionic concentration influenced the sensitivity of MST3 activity. Taken together, our data suggests that the serine/threonine kinase MST3 undergoes tyrosinedirected phosphorylation. The tyrosine-phosphorylated MST3 may create a docking site for the structurally conserved SH2/SH3 (Src Homology 2 and 3) domains within the Src oncoprotein. The unusual tyrosinephosphorylated MST3 may recruit MST3 to various signaling components.

Original languageEnglish
Pages (from-to)33-39
Number of pages7
JournalJournal of Inorganic Biochemistry
Volume160
DOIs
Publication statusPublished - 2016 Jul 1

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Phosphorylation
Phosphotransferases
Chemical activation
Yeast
Tyrosine
Yeasts
Mitogen-Activated Protein Kinases
Protein-Serine-Threonine Kinases
GTP-Binding Proteins
Protein Kinases
Vertebrates
pervanadate
3-tyrosine
Pheromone Receptors
MAP Kinase Kinase Kinases
Cell Polarity
Protein Conformation
Mammals
Pheromones
Oncogene Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

Kan, Wei Chih ; Lu, Te Ling ; Ling, Pin ; Lee, Te Hsiu ; Cho, Chien Yu ; Huang, Chi Ying F. ; Jeng, Wen-Yih ; Weng, Yui Ping ; Chiang, Chun Yen ; Wu, Jin Bin ; Lu, Te Jung. / Pervanadate induces Mammalian Ste20 Kinase 3 (MST3) tyrosine phosphorylation but not activation. In: Journal of Inorganic Biochemistry. 2016 ; Vol. 160. pp. 33-39.
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Pervanadate induces Mammalian Ste20 Kinase 3 (MST3) tyrosine phosphorylation but not activation. / Kan, Wei Chih; Lu, Te Ling; Ling, Pin; Lee, Te Hsiu; Cho, Chien Yu; Huang, Chi Ying F.; Jeng, Wen-Yih; Weng, Yui Ping; Chiang, Chun Yen; Wu, Jin Bin; Lu, Te Jung.

In: Journal of Inorganic Biochemistry, Vol. 160, 01.07.2016, p. 33-39.

Research output: Contribution to journalArticle

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AU - Kan, Wei Chih

AU - Lu, Te Ling

AU - Ling, Pin

AU - Lee, Te Hsiu

AU - Cho, Chien Yu

AU - Huang, Chi Ying F.

AU - Jeng, Wen-Yih

AU - Weng, Yui Ping

AU - Chiang, Chun Yen

AU - Wu, Jin Bin

AU - Lu, Te Jung

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