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MYOM1

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MYOM1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMYOM1, SKELEMIN, myomesin 1
External IDsOMIM: 603508; MGI: 1341430; HomoloGene: 31196; GeneCards: MYOM1; OMA:MYOM1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

8736

17929

Ensembl

ENSG00000101605

ENSMUSG00000024049

UniProt

P52179

Q62234

RefSeq (mRNA)

NM_003803
NM_019856

NM_001083934
NM_010867

RefSeq (protein)

NP_003794
NP_062830

NP_001077403
NP_034997

Location (UCSC)Chr 18: 3.07 – 3.22 MbChr 17: 71.31 – 71.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myomesin-1 is a protein that in humans is encoded by the MYOM1 gene.[5][6] Myomesin-1 is expressed in muscle cells and functions to stabilize the three-dimensional conformation of the thick filament. Embryonic forms of Myomesin-1 have been detected in dilated cardiomyopathy.

Structure

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Alternatively spliced variants of MYOM1, including EH-myomesin,[7] Skelemin[8] and Myomesin-1[8][9][10] have been identified; with Skelemin having an additional 96 amino acids rich in serine and proline residues.[8] Myomesin-1, like myomesin 2 and titin, is a member of a family of myosin-associated proteins containing structural modules with strong homology to either fibronectin type III (motif I) or immunoglobulin C2 (motif II) domains. Myomesin-1 bears uniqueness within this family in that it has intermediate filament core-like motifs, one near each terminus.[11] Myomesin-1 and Myomesin-2 each have a unique N-terminal region followed by 12 modules of motif I or motif II, in the arrangement II-II-I-I-I-I-I-II-II-II-II-II. The two proteins share 50% sequence identity in this repeat-containing region. The head structure formed by these 2 proteins on one end of the titin string extends into the center of the M band. Alternatively spliced, tissue-specific transcript variants encoding different isoforms have been identified.[12] Myomesin-1 can dimerize in an anti-parallel fashion via its C-terminal region.[13]

Function

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Titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line, where it binds tightly to Myomesin-1 and myomesin 2. Skelemin/Myomesin-1 is concentrated at peripheral regions of M-bands, and is postulated to link myofibrils with the intermediate filament cytoskeleton.[11] Skelemin/Myomesin-1 has been detected in the nucleus as well as the cytoskeletal, suggesting that it may play a role in gene expression.[14] Myomesin-1 functions to mediate stretch-induced signaling,[15] and the EH-myomesin splice variant, expressed in embryonic hearts and in dilated cardiomyopathy, can modulate its elasticity.[16]

Clinical Significance

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The fetal EH-myomesin alternatively spliced form of MYOM1 has been shown to be reexpressed at an early timepoint in the progression of dilated cardiomyopathy, coincident with isoform switches in titin.[17]

MYOM1 has also been shown to be abnormally spliced in patients with myotonic dystrophy type I; specifically, exon 17a.[18]

Interactions

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Skelemin/Myomesin-1 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101605 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024049 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Speel EJ, van der Ven PF, Albrechts JC, Ramaekers FC, Fürst DO, Hopman AH (Nov 1998). "Assignment of the human gene for the sarcomeric M-band protein myomesin (MYOM1) to 18p11.31-p11.32". Genomics. 54 (1): 184–6. doi:10.1006/geno.1998.5503. PMID 9806852.
  6. ^ "Entrez Gene: MYOM1 myomesin 1 (skelemin) 185kDa".
  7. ^ Agarkova I, Auerbach D, Ehler E, Perriard JC (Apr 2000). "A novel marker for vertebrate embryonic heart, the EH-myomesin isoform". The Journal of Biological Chemistry. 275 (14): 10256–64. doi:10.1074/jbc.275.14.10256. PMID 10744711.
  8. ^ a b c Steiner F, Weber K, Fürst DO (Feb 1999). "M band proteins myomesin and skelemin are encoded by the same gene: analysis of its organization and expression". Genomics. 56 (1): 78–89. doi:10.1006/geno.1998.5682. PMID 10036188.
  9. ^ "Protein sequence of human MYOM1 (Uniprot ID: P52179)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 24 June 2015. Retrieved 24 June 2015.
  10. ^ "Protein sequence of human MYOM1 (Uniprot ID: P52179-2)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 24 June 2015. Retrieved 24 June 2015.
  11. ^ a b Price MG, Gomer RH (Oct 1993). "Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins". The Journal of Biological Chemistry. 268 (29): 21800–10. doi:10.1016/S0021-9258(20)80613-9. PMID 8408035.
  12. ^ Bantle S, Keller S, Haussmann I, Auerbach D, Perriard E, Mühlebach S, Perriard JC (Aug 1996). "Tissue-specific isoforms of chicken myomesin are generated by alternative splicing". The Journal of Biological Chemistry. 271 (32): 19042–52. doi:10.1074/jbc.271.32.19042. PMID 8702575.
  13. ^ Lange S, Himmel M, Auerbach D, Agarkova I, Hayess K, Fürst DO, Perriard JC, Ehler E (Jan 2005). "Dimerisation of myomesin: implications for the structure of the sarcomeric M-band". Journal of Molecular Biology. 345 (2): 289–98. doi:10.1016/j.jmb.2004.10.040. PMID 15571722.
  14. ^ Reddy KB, Fox JE, Price MG, Kulkarni S, Gupta S, Das B, Smith DM (2008). "Nuclear localization of Myomesin-1: possible functions". Journal of Muscle Research and Cell Motility. 29 (1): 1–8. doi:10.1007/s10974-008-9137-x. PMID 18521710. S2CID 12298270.
  15. ^ Agarkova I, Perriard JC (Sep 2005). "The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere". Trends in Cell Biology. 15 (9): 477–85. CiteSeerX 10.1.1.384.2007. doi:10.1016/j.tcb.2005.07.001. PMID 16061384.
  16. ^ Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I (Jun 2005). "Myomesin is a molecular spring with adaptable elasticity". Journal of Molecular Biology. 349 (2): 367–79. doi:10.1016/j.jmb.2005.03.055. PMID 15890201.
  17. ^ Schoenauer R, Emmert MY, Felley A, Ehler E, Brokopp C, Weber B, Nemir M, Faggian GG, Pedrazzini T, Falk V, Hoerstrup SP, Agarkova I (Mar 2011). "EH-myomesin splice isoform is a novel marker for dilated cardiomyopathy". Basic Research in Cardiology. 106 (2): 233–47. doi:10.1007/s00395-010-0131-2. PMC 3032906. PMID 21069531.
  18. ^ Koebis M, Ohsawa N, Kino Y, Sasagawa N, Nishino I, Ishiura S (Sep 2011). "Alternative splicing of myomesin 1 gene is aberrantly regulated in myotonic dystrophy type 1". Genes to Cells. 16 (9): 961–72. doi:10.1111/j.1365-2443.2011.01542.x. PMID 21794030. S2CID 3272510.
  19. ^ a b Reddy KB, Gascard P, Price MG, Negrescu EV, Fox JE (Dec 1998). "Identification of an interaction between the m-band protein skelemin and beta-integrin subunits. Colocalization of a skelemin-like protein with beta1- and beta3-integrins in non-muscle cells". The Journal of Biological Chemistry. 273 (52): 35039–47. doi:10.1074/jbc.273.52.35039. PMID 9857037.
  20. ^ a b Deshmukh L, Tyukhtenko S, Liu J, Fox JE, Qin J, Vinogradova O (Nov 2007). "Structural insight into the interaction between platelet integrin alphaIIbbeta3 and cytoskeletal protein skelemin". The Journal of Biological Chemistry. 282 (44): 32349–56. doi:10.1074/jbc.M704666200. PMID 17804417.
  21. ^ a b Obermann WM, Gautel M, Weber K, Fürst DO (Jan 1997). "Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin". The EMBO Journal. 16 (2): 211–20. doi:10.1093/emboj/16.2.211. PMC 1169628. PMID 9029142.
  22. ^ Obermann WM, van der Ven PF, Steiner F, Weber K, Fürst DO (Apr 1998). "Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band". Molecular Biology of the Cell. 9 (4): 829–40. doi:10.1091/mbc.9.4.829. PMC 25310. PMID 9529381.
  23. ^ Auerbach D, Bantle S, Keller S, Hinderling V, Leu M, Ehler E, Perriard JC (May 1999). "Different domains of the M-band protein myomesin are involved in myosin binding and M-band targeting". Molecular Biology of the Cell. 10 (5): 1297–308. doi:10.1091/mbc.10.5.1297. PMC 25262. PMID 10233145.
  24. ^ Li TB, Liu XH, Feng S, Hu Y, Yang WX, Han Y, Wang YG, Gong LM (Jun 2004). "Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle" (PDF). Acta Biochimica et Biophysica Sinica. 36 (6): 412–8. doi:10.1093/abbs/36.6.412. PMID 15188056. S2CID 18331104. Archived from the original (PDF) on 2019-02-22.

Further reading

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