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

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 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 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

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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