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CLK1  -  CDC-like kinase 1

Homo sapiens

 
 
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High impact information on CLK1

 

Biological context of CLK1

  • CLK1 phosphorylation of YPTP1 led to a 3-fold stimulation of phosphatase activity in vitro [4].
  • The eukaryotic LAMMER protein kinase family is encoded by at least three loci in the human genome, designated CLK1, 2, and 3 [5].
  • The suppressed genes include mainly cell cycle regulators like cyclin B1, cyclin H and kinases like c-abl, CLK1 and others [6].
  • The suppressing mutation maps to the 3' end of a gene, masK, in an operon immediately upstream of the mglBA operon. masK encodes a protein of the STY kinase family [7].
  • However, the actual cellular mechanism that regulates cell growth, differentiation, and development by CLK/STY remains unclear [8].
 

Anatomical context of CLK1

  • CLK1 mRNA is expressed at low levels in all tissues and cell lines examined [9].
  • STY is a murine LAMMER kinase which has been implicated in the control of PC12 cell differentiation [10].
  • We have compared the expression patterns of these proteins in mouse tissues and transformed cell lines with that of a previously cloned family member (mCLK1/STY), and detected various transcripts for each gene [11].
  • The deduced amino acid sequence and the data from immunostaining of CL-K1 cDNA expressing CHO cells revealed that CL-K1 is expressed as a secreted protein [12].
 

Associations of CLK1 with chemical compounds

 

Regulatory relationships of CLK1

  • These findings demonstrate that the CLK kinases activate PTP-1B family members, and this phosphatase may be an important cellular target for CLK action [4].
 

Other interactions of CLK1

  • Co-expression of CLK1 or CLK2 with PTP-1B in HEK 293 cells led to a 2-fold stimulation of phosphatase activity in vivo [4].
  • Enzymes that phosphorylate the SR proteins belong to the family of CDC2/CDC28-like kinases (CLK) [14].
  • A benzothiazole compound TG003, a kinase inhibitor that targets Clk1 and Clk4, suppressed dissociation of nuclear speckles, altered the splicing patterns, and rescued the embryonic defects induced by excessive Clk activity [15].
 

Analytical, diagnostic and therapeutic context of CLK1

References

  1. Manipulation of alternative splicing by a newly developed inhibitor of Clks. Muraki, M., Ohkawara, B., Hosoya, T., Onogi, H., Koizumi, J., Koizumi, T., Sumi, K., Yomoda, J., Murray, M.V., Kimura, H., Furuichi, K., Shibuya, H., Krainer, A.R., Suzuki, M., Hagiwara, M. J. Biol. Chem. (2004) [Pubmed]
  2. Mutational analysis of stress-responsive peanut dual specificity protein kinase. Identification of tyrosine residues involved in regulation of protein kinase activity. Rudrabhatla, P., Rajasekharan, R. J. Biol. Chem. (2003) [Pubmed]
  3. Cloning of human PRP4 reveals interaction with Clk1. Kojima, T., Zama, T., Wada, K., Onogi, H., Hagiwara, M. J. Biol. Chem. (2001) [Pubmed]
  4. The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. Moeslein, F.M., Myers, M.P., Landreth, G.E. J. Biol. Chem. (1999) [Pubmed]
  5. Chromosomal mapping of three human LAMMER protein-kinase-encoding genes. Talmadge, C.B., Finkernagel, S., Sumegi, J., Sciorra, L., Rabinow, L. Hum. Genet. (1998) [Pubmed]
  6. Profile of gene expression regulated by induced p53: connection to the TGF-beta family. Kannan, K., Amariglio, N., Rechavi, G., Givol, D. FEBS Lett. (2000) [Pubmed]
  7. MglA, a small GTPase, interacts with a tyrosine kinase to control type IV pili-mediated motility and development of Myxococcus xanthus. Thomasson, B., Link, J., Stassinopoulos, A.G., Burke, N., Plamann, L., Hartzell, P.L. Mol. Microbiol. (2002) [Pubmed]
  8. The kic1 kinase of schizosaccharomyces pombe is a CLK/STY orthologue that regulates cell-cell separation. Tang, Z., Mandel, L.L., Yean, S.L., Lin, C.X., Chen, T., Yanagida, M., Lin, R.J. Exp. Cell Res. (2003) [Pubmed]
  9. Biochemical characterization and localization of the dual specificity kinase CLK1. Menegay, H.J., Myers, M.P., Moeslein, F.M., Landreth, G.E. J. Cell. Sci. (2000) [Pubmed]
  10. Alternative splicing of STY, a nuclear dual specificity kinase. Duncan, P.I., Howell, B.W., Marius, R.M., Drmanic, S., Douville, E.M., Bell, J.C. J. Biol. Chem. (1995) [Pubmed]
  11. Characterization and comparison of four serine- and arginine-rich (SR) protein kinases. Nayler, O., Stamm, S., Ullrich, A. Biochem. J. (1997) [Pubmed]
  12. Identification and Characterization of a Novel Human Collectin CL-K1. Keshi, H., Sakamoto, T., Kawai, T., Ohtani, K., Katoh, T., Jang, S.J., Motomura, W., Yoshizaki, T., Fukuda, M., Koyama, S., Fukuzawa, J., Fukuoh, A., Yoshida, I., Suzuki, Y., Wakamiya, N. Microbiol. Immunol. (2006) [Pubmed]
  13. Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A. Umehara, H., Nishii, Y., Morishima, M., Kakehi, Y., Kioka, N., Amachi, T., Koizumi, J., Hagiwara, M., Ueda, K. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  14. Molecular characterization of a cDNA encoding functional human CLK4 kinase and localization to chromosome 5q35 [correction of 4q35]. Schultz, J., Jones, T., Bork, P., Sheer, D., Blencke, S., Steyrer, S., Wellbrock, U., Bevec, D., Ullrich, A., Wallasch, C. Genomics (2001) [Pubmed]
  15. Alternative splicing: a new drug target of the post-genome era. Hagiwara, M. Biochim. Biophys. Acta (2005) [Pubmed]
  16. Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing. Sacco-Bubulya, P., Spector, D.L. J. Cell Biol. (2002) [Pubmed]
  17. Functional characterization of peanut serine/threonine/tyrosine protein kinase: molecular docking and inhibition kinetics with tyrosine kinase inhibitors. Rudrabhatla, P., Rajasekharan, R. Biochemistry (2004) [Pubmed]
  18. clk1, a serine/threonine protein kinase-encoding gene, is involved in pathogenicity of Colletotrichum lindemuthianum on common bean. Dufresne, M., Bailey, J.A., Dron, M., Langin, T. Mol. Plant Microbe Interact. (1998) [Pubmed]
 
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