LIMK2

From Wikipedia, the free encyclopedia


LIM domain kinase 2
PDB rendering based on 1x6a.
Available structures: 1x6a
Identifiers
Symbol(s) LIMK2;
External IDs OMIM: 601988 MGI1197517 HomoloGene55911
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 3985 16886
Ensembl ENSG00000182541 ENSMUSG00000020451
Uniprot P53671 Q5NC04
Refseq NM_001031801 (mRNA)
NP_001026971 (protein)
NM_001034030 (mRNA)
NP_001029202 (protein)
Location Chr 22: 29.94 - 30.01 Mb Chr 11: 3.24 - 3.31 Mb
Pubmed search [1] [2]

LIM domain kinase 2, also known as LIMK2, is a human gene.[1]

There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. The protein encoded by this gene is phosphorylated and activated by ROCK, a downstream effector of Rho, and the encoded protein, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the actin cytoskeleton. At least three transcript variants encoding different isoforms have been found for this gene.[1]

[edit] References

[edit] Further reading

  • Scott RW, Olson MF (2007). "LIM kinases: function, regulation and association with human disease.". J. Mol. Med. 85 (6): 555–68. doi:10.1007/s00109-007-0165-6. PMID 17294230. 
  • Okano I, Hiraoka J, Otera H, et al. (1996). "Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs.". J. Biol. Chem. 270 (52): 31321–30. PMID 8537403. 
  • Osada H, Hasada K, Inazawa J, et al. (1997). "Subcellular localization and protein interaction of the human LIMK2 gene expressing alternative transcripts with tissue-specific regulation.". Biochem. Biophys. Res. Commun. 229 (2): 582–9. doi:10.1006/bbrc.1996.1847. PMID 8954941. 
  • Hiraoka J, Okano I, Higuchi O, et al. (1997). "Self-association of LIM-kinase 1 mediated by the interaction between an N-terminal LIM domain and a C-terminal kinase domain.". FEBS Lett. 399 (1-2): 117–21. PMID 8980133. 
  • Yang N, Higuchi O, Ohashi K, et al. (1998). "Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization.". Nature 393 (6687): 809–12. doi:10.1038/31735. PMID 9655398. 
  • Nomoto S, Tatematsu Y, Takahashi T, Osada H (1999). "Cloning and characterization of the alternative promoter regions of the human LIMK2 gene responsible for alternative transcripts with tissue-specific expression.". Gene 236 (2): 259–71. PMID 10452946. 
  • Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22.". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208. 
  • Sumi T, Matsumoto K, Takai Y, Nakamura T (2000). "Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2.". J. Cell Biol. 147 (7): 1519–32. PMID 10613909. 
  • Sumi T, Matsumoto K, Nakamura T (2001). "Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase.". J. Biol. Chem. 276 (1): 670–6. doi:10.1074/jbc.M007074200. PMID 11018042. 
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination.". Genome Res. 10 (11): 1788–95. PMID 11076863. 
  • Amano T, Tanabe K, Eto T, et al. (2001). "LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505.". Biochem. J. 354 (Pt 1): 149–59. PMID 11171090. 
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166. 
  • Sumi T, Matsumoto K, Shibuya A, Nakamura T (2001). "Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha.". J. Biol. Chem. 276 (25): 23092–6. doi:10.1074/jbc.C100196200. PMID 11340065. 
  • Toshima J, Toshima JY, Takeuchi K, et al. (2001). "Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells.". J. Biol. Chem. 276 (33): 31449–58. doi:10.1074/jbc.M102988200. PMID 11418599. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMID 15231748. 
  • Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome.". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMID 15461802. 
  • Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline.". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMID 15489336. 
  • Vardouli L, Moustakas A, Stournaras C (2005). "LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-beta.". J. Biol. Chem. 280 (12): 11448–57. doi:10.1074/jbc.M402651200. PMID 15647284.