LIMK1

From Wikipedia, the free encyclopedia

LIM domain kinase 1

Identifiers

External IDs

OMIM: 601329 MGI: 104572 HomoloGene: 1738

Gene ontology
Molecular Function:	• nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein-tyrosine kinase activity • protein binding • ATP binding • zinc ion binding • transferase activity • metal ion binding • protein heterodimerization activity
Cellular Component:	• nucleus • cytoplasm • focal adhesion
Biological Process:	• protein amino acid phosphorylation • cell motility • signal transduction • Rho protein signal transduction • nervous system development • actin cytoskeleton organization and biogenesis • positive regulation of axon extension

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002314 (mRNA)
NP_002305 (protein)

NM_010717 (mRNA)
NP_034847 (protein)

Location

Chr 7: 73.14 - 73.17 Mb

Chr 5: 134.94 - 134.97 Mb

Pubmed search

[1]

[2]

LIM domain kinase 1, also known as LIMK1, is a human gene.

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. LIMK1 is likely to be a component of an intracellular signaling pathway and may be involved in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome.^[1]

[edit] References

^ Entrez Gene: LIMK1 LIM domain kinase 1.

[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.
Mizuno K, Okano I, Ohashi K, et al. (1994). "Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif.". Oncogene 9 (6): 1605–12. PMID 8183554.
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.
Tassabehji M, Metcalfe K, Fergusson WD, et al. (1996). "LIM-kinase deleted in Williams syndrome.". Nat. Genet. 13 (3): 272–3. doi:10.1038/ng0796-272. PMID 8673124.
Frangiskakis JM, Ewart AK, Morris CA, et al. (1996). "LIM-kinase1 hemizygosity implicated in impaired visuospatial constructive cognition.". Cell 86 (1): 59–69. PMID 8689688.
Osborne LR, Martindale D, Scherer SW, et al. (1997). "Identification of genes from a 500-kb region at 7q11.23 that is commonly deleted in Williams syndrome patients.". Genomics 36 (2): 328–36. doi:10.1006/geno.1996.0469. PMID 8812460.
Nebl G, Meuer SC, Samstag Y (1996). "Dephosphorylation of serine 3 regulates nuclear translocation of cofilin.". J. Biol. Chem. 271 (42): 26276–80. PMID 8824278.
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.
Wang JY, Frenzel KE, Wen D, Falls DL (1998). "Transmembrane neuregulins interact with LIM kinase 1, a cytoplasmic protein kinase implicated in development of visuospatial cognition.". J. Biol. Chem. 273 (32): 20525–34. PMID 9685409.
Edwards DC, Gill GN (1999). "Structural features of LIM kinase that control effects on the actin cytoskeleton.". J. Biol. Chem. 274 (16): 11352–61. PMID 10196227.
Sotiropoulos A, Gineitis D, Copeland J, Treisman R (1999). "Signal-regulated activation of serum response factor is mediated by changes in actin dynamics.". Cell 98 (2): 159–69. PMID 10428028.
Bach I, Rodriguez-Esteban C, Carrière C, et al. (1999). "RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex.". Nat. Genet. 22 (4): 394–9. doi:10.1038/11970. PMID 10431247.
Maekawa M, Ishizaki T, Boku S, et al. (1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase.". Science 285 (5429): 895–8. PMID 10436159.
Edwards DC, Sanders LC, Bokoch GM, Gill GN (1999). "Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.". Nat. Cell Biol. 1 (5): 253–9. doi:10.1038/12963. PMID 10559936.
Ohashi K, Nagata K, Maekawa M, et al. (2000). "Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop.". J. Biol. Chem. 275 (5): 3577–82. PMID 10652353.
Martindale DW, Wilson MD, Wang D, et al. (2000). "Comparative genomic sequence analysis of the Williams syndrome region (LIMK1-RFC2) of human chromosome 7q11.23.". Mamm. Genome 11 (10): 890–8. PMID 11003705.
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.
Dan C, Kelly A, Bernard O, Minden A (2001). "Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin.". J. Biol. Chem. 276 (34): 32115–21. doi:10.1074/jbc.M100871200. PMID 11413130.
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.