Expression of the Stp1 LMW-PTP and inhibition of protein CK2 display a cooperative effect on immunophilin Fpr3 tyrosine phosphorylation and Saccharomyces cerevisiae growth

M Marchetta; T Gamberi; S Sarno; F Magherini; G Raugei; G Camici; L A Pinna; A Modesti

doi:10.1007/s00018-004-4019-x

Expression of the Stp1 LMW-PTP and inhibition of protein CK2 display a cooperative effect on immunophilin Fpr3 tyrosine phosphorylation and Saccharomyces cerevisiae growth

Cell Mol Life Sci. 2004 May;61(10):1176-84. doi: 10.1007/s00018-004-4019-x.

Authors

M Marchetta¹, T Gamberi, S Sarno, F Magherini, G Raugei, G Camici, L A Pinna, A Modesti

Affiliation

¹ Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale G. Morgagni 50, 50134 Firenze, Italy.

Abstract

Although the yeast genome does not encode bona fide protein tyrosine kinases, tyrosine-phosphorylated proteins are numerous, suggesting that besides dual-specificity kinases, some Ser/Thr kinases are also committed to tyrosine phosphorylation in Saccharomyces cerevisiae. Here we show that blockage of the highly pleiotropic Ser/Thr kinase CK2 with a specific inhibitor synergizes with the overexpression of Stp1 low-molecular-weight protein tyrosine phosphatase (PTP) in inducing a severe growth-defective phenotype, consistent with a prominent role for CK2 in tyrosine phosphorylation in yeast. We also present in vivo evidence that immunophilin Fpr3, the only tyrosine-phosphorylated CK2 substrate recognized so far, interacts with and is dephosphorylated by Spt1. These data disclose a functional correlation between CK2 and LMW-PTPs, and suggest that reversible phosphorylation of Fpr3 plays a role in the regulation of growth rate and budding in S. cerevisiae.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Casein Kinase II
Cell Cycle
Cell Division
Enzyme Inhibitors / pharmacology
Immunoblotting
Immunophilins / metabolism*
Nuclear Proteins / biosynthesis*
Nuclear Proteins / physiology
Phenotype
Phosphorylation
Plasmids / metabolism
Precipitin Tests
Protein Serine-Threonine Kinases / antagonists & inhibitors*
RNA-Binding Proteins / biosynthesis*
RNA-Binding Proteins / physiology
Saccharomyces cerevisiae / metabolism*
Saccharomyces cerevisiae Proteins / biosynthesis*
Saccharomyces cerevisiae Proteins / metabolism*
Saccharomyces cerevisiae Proteins / physiology
Time Factors
Transcription Factors / biosynthesis*
Transcription Factors / physiology
Triazoles / pharmacology
Tyrosine / metabolism

Substances

4,5,6,7-tetrabromobenzotriazole
Enzyme Inhibitors
Nuclear Proteins
RNA-Binding Proteins
STP1 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
Transcription Factors
Triazoles
Tyrosine
Casein Kinase II
Protein Serine-Threonine Kinases
FPR3 protein, S cerevisiae
Immunophilins