MYOT

From Wikipedia, the free encyclopedia

Myotilin

Identifiers

MYOT; LGMD1; TTID

External IDs

OMIM: 604103 MGI: 1889800 HomoloGene: 4942

Gene ontology
Molecular Function:	• actin binding • protein binding • structural constituent of muscle
Cellular Component:	• actin cytoskeleton
Biological Process:	• muscle contraction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006790 (mRNA)
NP_006781 (protein)

NM_001033621 (mRNA)
NP_001028793 (protein)

Location

Chr 5: 137.23 - 137.25 Mb

Chr 18: 44.46 - 44.48 Mb

Pubmed search

[1]

[2]

Myotilin, also known as MYOT, is a human gene.^[1]

Striated muscle sarcomeres are highly organized structures composed of actin (thin) and myosin (thick) filaments that slide past each other during contraction. The integrity of sarcomeres is controlled by a set of structural proteins, among which are titin (TTN; MIM 188840), a giant molecule that contains several immunoglobulin (Ig)-like domains and associates with thin and thick filaments, and alpha-actinin (ACTN1; MIM 102575), an actin cross-linking protein. Mutations in several sarcomeric and sarcolemmal proteins have been shown to result in muscular dystrophy and cardiomyopathy.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: MYOT myotilin.

[edit] Further reading

Speer MC, Yamaoka LH, Gilchrist JH, et al. (1992). "Confirmation of genetic heterogeneity in limb-girdle muscular dystrophy: linkage of an autosomal dominant form to chromosome 5q.". Am. J. Hum. Genet. 50 (6): 1211–7. PMID 1598902.
Dixon MJ, Read AP, Donnai D, et al. (1991). "The gene for Treacher Collins syndrome maps to the long arm of chromosome 5.". Am. J. Hum. Genet. 49 (1): 17–22. PMID 1676560.
Bartoloni L, Horrigan SK, Viles KD, et al. (1999). "Use of a CEPH meiotic breakpoint panel to refine the locus of limb-girdle muscular dystrophy type 1A (LGMD1A) to a 2-Mb interval on 5q31.". Genomics 54 (2): 250–5. doi:10.1006/geno.1998.5579. PMID 9828127.
Salmikangas P, Mykkänen OM, Grönholm M, et al. (1999). "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy.". Hum. Mol. Genet. 8 (7): 1329–36. PMID 10369880.
Godley LA, Lai F, Liu J, et al. (1999). "TTID: A novel gene at 5q31 encoding a protein with titin-like features.". Genomics 60 (2): 226–33. doi:10.1006/geno.1999.5912. PMID 10486214.
Hauser MA, Horrigan SK, Salmikangas P, et al. (2000). "Myotilin is mutated in limb girdle muscular dystrophy 1A.". Hum. Mol. Genet. 9 (14): 2141–7. PMID 10958653.
van der Ven PF, Wiesner S, Salmikangas P, et al. (2000). "Indications for a novel muscular dystrophy pathway. gamma-filamin, the muscle-specific filamin isoform, interacts with myotilin.". J. Cell Biol. 151 (2): 235–48. PMID 11038172.
Hauser MA, Conde CB, Kowaljow V, et al. (2003). "myotilin Mutation found in second pedigree with LGMD1A.". Am. J. Hum. Genet. 71 (6): 1428–32. PMID 12428213.
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.
Salmikangas P, van der Ven PF, Lalowski M, et al. (2003). "Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly.". Hum. Mol. Genet. 12 (2): 189–203. PMID 12499399.
Battle MA, Maher VM, McCormick JJ (2003). "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways.". Biochemistry 42 (24): 7270–82. doi:10.1021/bi034081y. PMID 12809483.
Selcen D, Engel AG (2004). "Mutations in myotilin cause myofibrillar myopathy.". Neurology 62 (8): 1363–71. PMID 15111675.
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. PMID 15489334.
Witt SH, Granzier H, Witt CC, Labeit S (2005). "MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination.". J. Mol. Biol. 350 (4): 713–22. doi:10.1016/j.jmb.2005.05.021. PMID 15967462.
Gontier Y, Taivainen A, Fontao L, et al. (2006). "The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins.". J. Cell. Sci. 118 (Pt 16): 3739–49. doi:10.1242/jcs.02484. PMID 16076904.
von Nandelstadh P, Grönholm M, Moza M, et al. (2005). "Actin-organising properties of the muscular dystrophy protein myotilin.". Exp. Cell Res. 310 (1): 131–9. doi:10.1016/j.yexcr.2005.06.027. PMID 16122733.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Foroud T, Pankratz N, Batchman AP, et al. (2006). "A mutation in myotilin causes spheroid body myopathy.". Neurology 65 (12): 1936–40. doi:10.1212/01.wnl.0000188872.28149.9a. PMID 16380616.
Garvey SM, Senderek J, Beckmann JS, et al. (2006). "Myotilin is not the causative gene for vocal cord and pharyngeal weakness with distal myopathy (VCPDM).". Ann. Hum. Genet. 70 (Pt 3): 414–6. doi:10.1111/j.1529-8817.2005.00252.x. PMID 16674563.
Pénisson-Besnier I, Talvinen K, Dumez C, et al. (2006). "Myotilinopathy in a family with late onset myopathy.". Neuromuscul. Disord. 16 (7): 427–31. doi:10.1016/j.nmd.2006.04.009. PMID 16793270.