LIMK1

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LIM domain kinase 1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols LIMK1 ; LIMK; LIMK-1
External IDs OMIM601329 MGI104572 HomoloGene1738 ChEMBL: 3836 GeneCards: LIMK1 Gene
EC number 2.7.11.1
RNA expression pattern
PBB GE LIMK1 208372 s at tn.png
PBB GE LIMK1 204357 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3984 16885
Ensembl ENSG00000106683 ENSMUSG00000029674
UniProt P53667 P53668
RefSeq (mRNA) NM_001204426 NM_010717
RefSeq (protein) NP_001191355 NP_034847
Location (UCSC) Chr 7:
73.5 – 73.54 Mb
Chr 5:
134.66 – 134.69 Mb
PubMed search [1] [2]

LIM domain kinase 1 is an enzyme that in humans is encoded by the LIMK1 gene.[1][2]

Function[edit]

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, a central PDZ domain, 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.[3]

Clinical signficance[edit]

LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome.[3]

Interactions[edit]

LIMK1 has been shown to interact with:

References[edit]

  1. ^ Tassabehji M, Metcalfe K, Fergusson W, Carette M, Dore J, Donnai D et al. (Aug 1996). "LIM-kinase deleted in Williams syndrome". Nat. Genet. 13 (3): 272–3. doi:10.1038/ng0796-272. PMID 8673124. 
  2. ^ Osborne L, Martindale D, Scherer S, Shi X, Huizenga J, Heng H et al. (Jan 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. 
  3. ^ a b "Entrez Gene: LIMK1 LIM domain kinase 1". 
  4. ^ Foletta V, Lim M, Soosairajah J, Kelly A, Stanley E, Shannon M et al. (September 2003). "Direct signaling by the BMP type II receptor via the cytoskeletal regulator LIMK1". J. Cell Biol. 162 (6): 1089–98. doi:10.1083/jcb.200212060. PMC 2172847. PMID 12963706. 
  5. ^ Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A et al. (August 1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159. 
  6. ^ Yokoo T, Toyoshima H, Miura M, Wang Y, Iida K, Suzuki H et al. (December 2003). "p57Kip2 regulates actin dynamics by binding and translocating LIM-kinase 1 to the nucleus". J. Biol. Chem. 278 (52): 52919–23. doi:10.1074/jbc.M309334200. PMID 14530263. 
  7. ^ Wang J, Frenzel K, Wen D, Falls D (August 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. doi:10.1074/jbc.273.32.20525. PMID 9685409. 
  8. ^ Edwards D, Sanders L, Bokoch G, Gill G (September 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. 
  9. ^ Dan C, Kelly A, Bernard O, Minden A (August 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. 
  10. ^ Birkenfeld J, Betz H, Roth D (January 2003). "Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta". Biochem. J. 369 (Pt 1): 45–54. doi:10.1042/BJ20021152. PMC 1223062. PMID 12323073. 

Further reading[edit]

  • Scott R, Olson M (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, Nunoue K, Kuma K, Miyata T 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, Nunoue K, Ohashi K, Iwashita S et al. (1995). "Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs". J. Biol. Chem. 270 (52): 31321–30. doi:10.1074/jbc.270.52.31321. PMID 8537403. 
  • Frangiskakis J, Ewart A, Morris C, Mervis C, Bertrand J, Robinson B et al. (1996). "LIM-kinase1 hemizygosity implicated in impaired visuospatial constructive cognition". Cell 86 (1): 59–69. doi:10.1016/S0092-8674(00)80077-X. PMID 8689688. 
  • Nebl G, Meuer S, Samstag Y (1996). "Dephosphorylation of serine 3 regulates nuclear translocation of cofilin". J. Biol. Chem. 271 (42): 26276–80. doi:10.1074/jbc.271.42.26276. PMID 8824278. 
  • Hiraoka J, Okano I, Higuchi O, Yang N, Mizuno K (1996). "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. doi:10.1016/S0014-5793(96)01303-8. PMID 8980133. 
  • Yang N, Higuchi O, Ohashi K, Nagata K, Wada A, Kangawa 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 J, Frenzel K, Wen D, Falls D (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. doi:10.1074/jbc.273.32.20525. PMID 9685409. 
  • Edwards D, Gill G (1999). "Structural features of LIM kinase that control effects on the actin cytoskeleton". J. Biol. Chem. 274 (16): 11352–61. doi:10.1074/jbc.274.16.11352. 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. doi:10.1016/S0092-8674(00)81011-9. PMID 10428028. 
  • Bach I, Rodriguez-Esteban C, Carrière C, Bhushan A, Krones A, Rose D 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, Watanabe N, Fujita A, Iwamatsu A et al. (1999). "Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase". Science 285 (5429): 895–8. doi:10.1126/science.285.5429.895. PMID 10436159. 
  • Edwards D, Sanders L, Bokoch G, Gill G (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, Ishizaki T, Narumiya S, Mizuno K (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. doi:10.1074/jbc.275.5.3577. PMID 10652353. 
  • Martindale D, Wilson M, Wang D, Burke R, Chen X, Duronio V 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. doi:10.1007/s003350010166. 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 J, Takeuchi K, Mori R, Mizuno K (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. 

External links[edit]