MYLK2

Myosin light chain kinase 2
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2LV6​, 3KF9​
Identifiers
Symbols	MYLK2 ; KMLC; MLCK; MLCK2; skMLCK
External IDs	OMIM: 606566 MGI: 2139434 HomoloGene: 13223 IUPHAR: 1553 ChEMBL: 2777 GeneCards: MYLK2 Gene
EC number	2.7.11.18
Gene ontology Molecular function • calmodulin-dependent protein kinase activity • myosin light chain kinase activity • protein binding • calmodulin binding • ATP binding Cellular component • nucleus • cytoplasm • sarcomere Biological process • striated muscle contraction • neuromuscular synaptic transmission • positive regulation of gene expression • skeletal muscle satellite cell differentiation • peptidyl-threonine phosphorylation • regulation of muscle filament sliding • skeletal muscle cell differentiation • protein autophosphorylation • cardiac muscle tissue morphogenesis • cardiac muscle contraction Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	85366	228785
Ensembl	ENSG00000101306	ENSMUSG00000027470
UniProt	Q9H1R3	Q8VCR8
RefSeq (mRNA)	NM_033118	NM_001081044
RefSeq (protein)	NP_149109	NP_001074513
Location (UCSC)	Chr 20: 31.82 – 31.83 Mb	Chr 2: 152.91 – 152.92 Mb
PubMed search

Myosin light chain kinase 2 also known as MYLK2 is an enzyme which in humans is encoded by the MYLK2 gene.^[1]

Function

This gene encodes a myosin light chain kinase, a calcium / calmodulin dependent enzyme, that is exclusively expressed in adult skeletal muscle.^[2] The MYLK2 gene expresses skMLCK more prevalently in fast twitch muscle fibers as compared to slow twitch muscle fibers. Calmodulin is composed of two terminal domains (N,C) each containing two E-F hand motifs that bind to Ca2+. Upon saturation of Ca2+, Calmodulin undergoes a conformation change allowing it to bind with a target protein such as skMLCK. An image depicting a similar complex (sdCen/skMLCK2) is shown under myosin light chain kinase. This binding to skMLCK increases the affinity of Ca2+ and ultimately leads to a sustained muscle action.^[3]

Clinical significance

Mutations in the MYLK2 gene have been linked to midventricular hypertrophic cardiomyopathy.^[1]

References

1. Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, Epstein ND (November 2001). "The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation". Cell 107 (5): 631–41. doi:10.1016/S0092-8674(01)00586-4. PMID 11733062.
2. "Entrez Gene: MYLK2 myosin light chain kinase 2, skeletal muscle".
3. Stull JT, Kamm KE, Vandenboom R (February 2011). "Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle". Arch Biochem Biophys 510 (2): 120–8. doi:10.1016/j.abb.2011.01.017. PMC 3101293. PMID 21284933.

Further reading

• Jeronimo C, Forget D, Bouchard A, et al. (2007). "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme.". Mol. Cell 27 (2): 262–74. doi:10.1016/j.molcel.2007.06.027. PMID 17643375.
• Junker JP, Rief M (2009). "Single-molecule force spectroscopy distinguishes target binding modes of calmodulin.". Proc. Natl. Acad. Sci. U.S.A. 106 (34): 14361–6. doi:10.1073/pnas.0904654106. PMC 2732892. PMID 19667195.
• Roush CL, Kennelly PJ, Glaccum MB, et al. (1988). "Isolation of the cDNA encoding rat skeletal muscle myosin light chain kinase. Sequence and tissue distribution.". J. Biol. Chem. 263 (21): 10510–6. PMID 2839493.
• Christie JD, Ma SF, Aplenc R, et al. (2008). "Variation in the myosin light chain kinase gene is associated with development of acute lung injury after major trauma.". Crit. Care Med. 36 (10): 2794–800. doi:10.1097/CCM.0b013e318186b843. PMID 18828194.
• Lazar V, Garcia JG (1999). "A single human myosin light chain kinase gene (MLCK; MYLK).". Genomics 57 (2): 256–67. doi:10.1006/geno.1999.5774. PMID 10198165.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
• Soung YH, Lee JW, Kim SY, et al. (2006). "Mutational analysis of the kinase domain of MYLK2 gene in common human cancers.". Pathol. Res. Pract. 202 (3): 137–40. doi:10.1016/j.prp.2005.12.003. PMID 16448786.
• Gallagher PJ, Herring BP, Stull JT (1997). "Myosin light chain kinases.". J. Muscle Res. Cell. Motil. 18 (1): 1–16. doi:10.1023/A:1018616814417. PMID 9147985.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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. PMC 139241. PMID 12477932.
• Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization.". Genome Res. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
• Toth-Zsamboki E, Oury C, Cornelissen H, et al. (2003). "P2X1-mediated ERK2 activation amplifies the collagen-induced platelet secretion by enhancing myosin light chain kinase activation.". J. Biol. Chem. 278 (47): 46661–7. doi:10.1074/jbc.M308452200. PMID 14500714.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.