scholarly journals Essential Functions of Protein Tyrosine Phosphatases Ptp2 and Ptp3 and Rim11 Tyrosine Phosphorylation inSaccharomyces cerevisiaeMeiosis and Sporulation

2000 ◽  
Vol 11 (2) ◽  
pp. 663-676 ◽  
Author(s):  
Xiao-Li Zhan ◽  
Yulong Hong ◽  
Tianqing Zhu ◽  
Aaron P. Mitchell ◽  
Robert J. Deschenes ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Map Kinases ◽  
Early Stage ◽  
Protein Tyrosine Phosphatases ◽  
Homozygous Deletion ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Biochemical Processes ◽  
Tyrosine Phosphorylated Protein

Tyrosine phosphorylation plays a central role in eukaryotic signal transduction. In yeast, MAP kinase pathways are regulated by tyrosine phosphorylation, and it has been speculated that other biochemical processes may also be regulated by tyrosine phosphorylation. Previous genetic and biochemical studies demonstrate that protein tyrosine phosphatases (PTPases) negatively regulate yeast MAP kinases. Here we report that deletion of PTP2 and PTP3results in a sporulation defect, suggesting that tyrosine phosphorylation is involved in regulation of meiosis and sporulation. Deletion of PTP2 and PTP3 blocks cells at an early stage of sporulation before premeiotic DNA synthesis and induction of meiotic-specific genes. We observed that tyrosine phosphorylation of several proteins, including 52-, 43-, and 42-kDa proteins, was changed in ptp2Δptp3Δ homozygous deletion cells under sporulation conditions. The 42-kDa tyrosine-phosphorylated protein was identified as Mck1, which is a member of the GSK3 family of protein kinases and previously known to be phosphorylated on tyrosine. Mutation of MCK1 decreases sporulation efficiency, whereas mutation of RIM11, another GSK3 member, specifically abolishes sporulation; therefore, we investigated regulation of Rim11 by Tyr phosphorylation during sporulation. We demonstrated that Rim11 is phosphorylated on Tyr-199, and the Tyr phosphorylation is essential for its in vivo function, although Rim11 appears not to be directly regulated by Ptp2 and Ptp3. Biochemical characterizations indicate that tyrosine phosphorylation of Rim11 is essential for the activity of Rim11 to phosphorylate substrates. Our data demonstrate important roles of protein tyrosine phosphorylation in meiosis and sporulation

scholarly journals SHP1 and SHP2 Protein-tyrosine Phosphatases Associate with βc after Interleukin-3-induced Receptor Tyrosine Phosphorylation

1997 ◽  
Vol 272 (22) ◽  
pp. 14470-14476 ◽  
Author(s):  
Heather Bone ◽  
Ute Dechert ◽  
Frank Jirik ◽  
John W. Schrader ◽  
Melanie J. Welham
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Interleukin 3

scholarly journals Podocyte Protein, Nephrin, Is a Substrate of Protein Tyrosine Phosphatase 1B

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Lamine Aoudjit ◽  
Ruihua Jiang ◽  
Tae Hoon Lee ◽  
Laura A. New ◽  
Nina Jones ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Protein Tyrosine Phosphatase 1B ◽  
Tyrosine Phosphatases ◽  
Puromycin Aminonucleoside ◽  
Protein Tyrosine ◽  
Aminonucleoside Nephrosis ◽  
Puromycin Aminonucleoside Nephrosis

Glomerular podocytes are critical for the barrier function of the glomerulus in the kidney and their dysfunction causes protein leakage into the urine (proteinuria). Nephrin is a key podocyte protein, which regulates the actin cytoskeleton via tyrosine phosphorylation of its cytoplasmic domain. Here we report that two protein tyrosine phosphatases, PTP1B and PTP-PEST negatively regulate nephrin tyrosine phosphorylation. PTP1B directly binds to and dephosphorylates nephrin, while the action of PTP-PEST is indirect. The two phosphatases are also upregulated in the glomerulus in the rat model of puromycin aminonucleoside nephrosis. Both overexpression and inhibition of PTP1B deranged the actin cytoskeleton in cultured mouse podocytes. Thus, protein tyrosine phosphatases may affect podocyte function via regulating nephrin tyrosine phosphorylation.

scholarly journals Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13.

1992 ◽  
Vol 12 (2) ◽  
pp. 836-846 ◽  
Author(s):  
T L Yi ◽  
J L Cleveland ◽  
J N Ihle
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Phosphatase ◽  
Human Gene ◽  
Tyrosine Phosphatase ◽  
Hematopoietic Cells ◽  
Protein Tyrosine Phosphatases ◽  
Hematopoietic Cell ◽  
Protein Tyrosine Phosphorylation ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We also cloned the human homolog, which has 95% amino acid sequence identity. Both the murine and human gene products have tyrosine-specific phosphatase activity, and both are expressed predominantly in hematopoietic cells. Importantly, the human gene maps to chromosome 12 region p12-p13. This region is associated with rearrangements in approximately 10% of cases of acute lymphocytic leukemia in children.

scholarly journals Differential regulation of the dual-specificity protein-tyrosine phosphatases CL100, B23, and PAC1 in mesangial cells.

1997 ◽  
Vol 8 (1) ◽  
pp. 40-50
Author(s):  
D Bokemeyer ◽  
A Sorokin ◽  
M J Dunn
Keyword(s):  
Map Kinase ◽  
Intracellular Signaling ◽  
Map Kinases ◽  
Mesangial Cells ◽  
Feedback Inhibition ◽  
Protein Tyrosine Phosphatases ◽  
P38 Map Kinase ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Dual Specificity

The extracellular-signal-regulated kinase (ERK), the best described MAP kinase cascade, is a major signaling system by which cells transduce extracellular cues into intracellular responses. ERK is activated by phosphorylation both on tyrosine and threonine residues. Therefore, a new clas of protein-tyrosine phosphatases (PTPases) that exhibit dual catalytic activity toward both regulatory sites on ERK is of special interest in the control of intracellular signaling. This study examined the expression and regulation of the dual-specificity PTPases CL100, B23, and PAC1. Findings included differential expression of these phosphatases in diverse cell lines and an expression of all three dual-specificity PTPases in human mesangial cells (HMC), thereby allowing investigation of their regulation in a single cell line. The MEK antagonist PD 098059 and selective extracellular agonists of ERK were used to demonstrate the induction of CL100, PAC1, and B23 in response to activation of the ERK cascade. In contrast, anisomycin, an agonist of the recently described MAP kinases stress-activated protein kinase (SAPK) and p38 MAP kinase, stimulated CL100 gene expression but had little effect on PAC1 and B23. This effect of anisomycin was partly inhibited in the presence of the p38 MAP kinase antagonist SB 203580. This study suggests a potential mechanism to regulate ERK activity through feedback inhibition by demonstrating the ERK cascade's induction of the dual-specificity PTPases CL100, PAC1, and B23. Moreover, this study suggests an ERK-independent induction of CL100 following stimulation of SAPK and p38 MAP kinase. This mode of induction of a phosphatase capable of inactivating ERK may play an important role in the cellular stress response.

Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains

2016 ◽  
Vol 44 (5) ◽  
pp. 1295-1303 ◽  
Author(s):  
Maayan Barnea ◽  
Tsviya Olender ◽  
Mark T. Bedford ◽  
Ari Elson
Keyword(s):  
Molecular Mechanisms ◽  
Protein Tyrosine Phosphatases ◽  
Cellular Function ◽  
Receptor Type ◽  
Tyrosine Phosphatases ◽  
Physiological Regulation ◽  
Protein Tyrosine ◽  
Physiological Conditions ◽  
Type Protein

Protein tyrosine phosphatases (PTPs) perform specific functions in vivo, despite being vastly outnumbered by their substrates. Because of this and due to the central roles PTPs play in regulating cellular function, PTP activity is regulated by a large variety of molecular mechanisms. We review evidence that indicates that the divergent C-terminal tail sequences (C-terminal domains, CTDs) of receptor-type PTPs (RPTPs) help regulate RPTP function by controlling intermolecular associations in a way that is itself subject to physiological regulation. We propose that the CTD of each RPTP defines an ‘interaction code’ that helps determine molecules it will interact with under various physiological conditions, thus helping to regulate and diversify PTP function.

An antibody-based method for monitoring in vivo oxidation of protein tyrosine phosphatases

Methods ◽  
2005 ◽  
Vol 35 (1) ◽  
pp. 37-43 ◽  
Author(s):  
C PERSSON ◽  
K KAPPERT ◽  
U ENGSTROM ◽  
A OSTMAN ◽  
T SJOBLOM
Keyword(s):  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine
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