scholarly journals CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity

FEBS Letters ◽  
2012 ◽  
Vol 586 (23) ◽  
pp. 4070-4075 ◽  
Author(s):  
Man-Ho Oh ◽  
Xia Wu ◽  
Hyoung Seok Kim ◽  
Jeffrey F. Harper ◽  
Raymond E. Zielinski ◽  
...  
Keyword(s):  
Protein Kinases ◽  
Kinase Activity ◽  
Dual Specificity ◽  
Specificity Protein ◽  
Tyrosine Autophosphorylation

scholarly journals Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity.

1994 ◽  
Vol 5 (8) ◽  
pp. 877-886 ◽  
Author(s):  
M F Hoekstra ◽  
N Dhillon ◽  
G Carmel ◽  
A J DeMaggio ◽  
R A Lindberg ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinases ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Tyrosine Kinase Activity ◽  
Casein Kinase I ◽  
Tyrosine Residues ◽  
Dual Specificity ◽  
Specificity Protein ◽  
Protein Tyrosine Kinase Activity

We have examined the activity and substrate specificity of the Saccharomyces cerevisiae Hrr25p and the Schizosaccharomyces pombe Hhp1, Hhp2, and Cki1 protein kinase isoforms. These four gene products are isotypes of casein kinase I (CKI), and the sequence of these protein kinases predicts that they are protein serine/threonine kinases. However, each of these four protein kinases, when expressed in Escherichia coli in an active form, was recognized by anti-phosphotyrosine antibodies. Phosphoamino acid analysis of 32P-labeled proteins showed phosphorylation on serine, threonine, and tyrosine residues. The E. coli produced forms of Hhp1, Hhp2, and Cki1 were autophosphorylated on tyrosine, and both Hhp1 and Hhp2 were capable of phosphorylating the tyrosine-protein kinase synthetic peptide substrate polymer poly-E4Y1. Immune complex protein kinases assays from S. pombe cells showed that Hhp1-containing precipitates were associated with a protein-tyrosine kinase activity, and the Hhp1 present in these immunoprecipitates was phosphorylated on tyrosine residues. Although dephosphorylation of Hhp1 and Hhp2 by Ser/Thr phosphatase had little effect on the specific activity, tyrosine dephosphorylation of Hhp1 and Hhp2 caused a 1.8-to 3.1-fold increase in the Km for poly-E4Y1 and casein. These data demonstrate that four different CKI isoforms from two different yeasts are capable of protein-tyrosine kinase activity and encode dual-specificity protein kinases.

scholarly journals Membrane localization of the kinase which phosphorylates p34cdc2 on threonine 14.

1994 ◽  
Vol 5 (3) ◽  
pp. 273-282 ◽  
Author(s):  
S Kornbluth ◽  
B Sebastian ◽  
T Hunter ◽  
J Newport
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Schizosaccharomyces Pombe ◽  
Protein Kinases ◽  
Membrane Fraction ◽  
Kinase Activity ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Dual Specificity ◽  
Detergent Extraction

The key regulator of entry into mitosis is the serine/threonine kinase p34cdc2. This kinase is regulated both by association with cyclins and by phosphorylation at several sites. Phosphorylation at Tyr 15 and Thr 14 are believed to inhibit the kinase activity of cdc2. In Schizosaccharomyces pombe, the wee1 (and possibly mik1) protein kinase catalyzes phosphorylation of Tyr 15. It is not clear whether these or other, as yet unidentified, protein kinases phosphorylate Thr 14. In this report we show, using extracts of Xenopus eggs, that the Thr 14-directed kinase is tightly membrane associated. Specifically, we have shown that a purified membrane fraction, in the absence of cytoplasm, can promote phosphorylation of cdc2 on both Thr 14 and Tyr 15. In contrast, the cytoplasm can phosphorylate cdc2 only on Tyr 15, suggesting the existence of at least two distinctly localized subpopulations of cdc2 Tyr 15-directed kinases. The membrane-associated Tyr 15 and Thr 14 kinase activities behaved similarly during salt or detergent extraction and were similarly regulated during the cell cycle and by the checkpoint machinery that delays mitosis while DNA is being replicated. This suggests the possibility that a dual-specificity membrane-associated protein kinase may catalyze phosphorylation of both Tyr 15 and Thr 14.

scholarly journals Unveiling the Novel Dual Specificity Protein Kinases inBacillus anthracis

2012 ◽  
Vol 287 (32) ◽  
pp. 26749-26763 ◽  
Author(s):  
Gunjan Arora ◽  
Andaleeb Sajid ◽  
Mary Diana Arulanandh ◽  
Anshika Singhal ◽  
Abid R. Mattoo ◽  
...  
Keyword(s):  
Protein Kinases ◽  
The Novel ◽  
Dual Specificity ◽  
Specificity Protein

scholarly journals The dual-specificity CLK kinase induces neuronal differentiation of PC12 cells.

1994 ◽  
Vol 14 (10) ◽  
pp. 6954-6961 ◽  
Author(s):  
M P Myers ◽  
M B Murphy ◽  
G Landreth
Keyword(s):  
Signal Transduction ◽  
Growth Factor ◽  
Protein Kinases ◽  
Pc12 Cells ◽  
Pc12 Cell ◽  
Morphological Differentiation ◽  
Signal Transduction Pathways ◽  
Dual Specificity ◽  
Free Media ◽  
Specificity Protein

CLK is a dual-specificity protein kinase capable of phosphorylating serine, threonine, and tyrosine residues. We have investigated the action of CLK by establishing stable PC12 cell lines capable of inducibly expressing CLK. Expression of CLK in stably transfected PC12 cells mimicked a number of nerve growth factor (NGF)-dependent events, including the morphological differentiation of these cells and the elaboration of neurites. Moreover, CLK expression enhanced the rate of NGF-mediated neurite outgrowth of these cells, indicating that CLK expression and NGF treatment activate similar signal transduction pathways. CLK expression, unlike NGF, was not able to promote PC12 cell survival in serum-free media, demonstrating that CLK only partially recapitulated the actions of NGF on these cells and that the biochemical pathways necessary for morphological differentiation can be stimulated without also stimulating those necessary for survival. Induction of CLK expression also resulted in the selective activation of protein kinases that are components of growth factor-stimulated signal transduction cascades, including ERK1, ERK2, pp90RSK, and S6PKII. Induction of CLK expression, however, did not stimulate pp70S6K or Fos kinase, two NGF-sensitive protein kinases. These data indicate that CLK action mediates the morphological differentiation of these cells through its capacity to independently stimulate signal transduction pathways normally employed by NGF.

scholarly journals DYRK1A Autophosphorylation on Serine Residue 520 Modulates Its Kinase Activity via 14-3-3 Binding

2007 ◽  
Vol 18 (4) ◽  
pp. 1167-1178 ◽  
Author(s):  
Mónica Alvarez ◽  
Xavier Altafaj ◽  
Sergi Aranda ◽  
Susana de la Luna
Keyword(s):  
Protein Kinases ◽  
Kinase Activity ◽  
Dynamic Changes ◽  
Activated T Cells ◽  
Cellular Processes ◽  
Dual Specificity ◽  
Evolutionarily Conserved ◽  
The Family ◽  
Intramolecular Mechanism

Dual-specificity tyrosine-phosphorylated and regulated kinase (DYRK) proteins are an evolutionarily conserved family of protein kinases, with members identified from yeast to humans, that participate in a variety of cellular processes. DYRKs are serine/threonine protein kinases that are activated by autophosphorylation on a tyrosine residue in the activation loop. The family member DYRK1A has been shown to phosphorylate several cytosolic proteins and a number of splicing and transcription factors, including members of the nuclear factor of activated T cells family. In the present study, we show that DYRK1A autophosphorylates, via an intramolecular mechanism, on Ser-520, in the PEST domain of the protein. We also show that phosphorylation of this residue, which we show is subjected to dynamic changes in vivo, mediates the interaction of DYRK1A with 14-3-3β. A second 14-3-3 binding site is present within the N-terminal of the protein. In the context of the DYRK1A molecule, neither site can act independently of the other. Bacterially produced DYRK1A and the mutant DYRK1A/S520A have similar kinase activities, suggesting that Ser-520 phosphorylation does not affect the intrinsic kinase activity on its own. Instead, we demonstrate that this phosphorylation allows the binding of 14-3-3β, which in turn stimulates the catalytic activity of DYRK1A. These findings provide evidence for a novel mechanism for the regulation of DYRK1A kinase activity.

The Clk2 and Clk3 Dual-Specificity Protein Kinases Regulate the Intranuclear Distribution of SR Proteins and Influence Pre-mRNA Splicing

1998 ◽  
Vol 241 (2) ◽  
pp. 300-308 ◽  
Author(s):  
Peter I. Duncan ◽  
David F. Stojdl ◽  
Ricardo M. Marius ◽  
Karl H. Scheit ◽  
John C. Bell
Keyword(s):  
Protein Kinases ◽  
Sr Proteins ◽  
Mrna Splicing ◽  
Dual Specificity ◽  
Specificity Protein

Dual-specificity protein kinases: will any hydroxyl do?

1992 ◽  
Vol 17 (3) ◽  
pp. 114-119 ◽  
Author(s):  
Richard A. Lindberg ◽  
Anne Marie Quinn ◽  
Tony Hunter
Keyword(s):  
Protein Kinases ◽  
Dual Specificity ◽  
Specificity Protein
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