MYLK2

MYLK2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LV6, 3KF9
Identifiers
Aliases	MYLK2, KMLC, MLCK, MLCK2, skMLCK, myosin light chain kinase 2
External IDs	MGI: 2139434 HomoloGene: 13223 GeneCards: MYLK2
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • calmodulin binding • myosin light chain kinase activity • kinase activity • protein serine/threonine kinase activity • protein binding • calmodulin-dependent protein kinase activity • ATP binding Cellular component • cytoplasm • sarcomere • nucleus Biological process • regulation of muscle filament sliding • cardiac muscle contraction • phosphorylation • cardiac muscle tissue morphogenesis • skeletal muscle satellite cell differentiation • protein phosphorylation • neuromuscular synaptic transmission • positive regulation of gene expression • skeletal muscle cell differentiation • protein autophosphorylation • peptidyl-threonine phosphorylation • striated 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_149109.1	NP_001074513.2
Location (UCSC)	Chr 20: 31.82 – 31.83 Mb	Chr 2: 152.91 – 152.92 Mb
PubMed search	[1]	[2]
Wikidata

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Myosin light chain kinase 2 also known as MYLK2 is an enzyme which in humans is encoded by the MYLK2 gene.^[3]

Function

This gene encodes a myosin light chain kinase, a calcium / calmodulin dependent enzyme, that is exclusively expressed in adult skeletal muscle.^[4] 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.^[5]

Clinical significance

Mutations in the MYLK2 gene have been linked to midventricular hypertrophic cardiomyopathy.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. "Entrez Gene: MYLK2 myosin light chain kinase 2, skeletal muscle".
5. 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 (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 (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 (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 (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 (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 (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 (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 (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 (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.