TPM1
From Wikipedia, the free encyclopedia
Tropomyosin alpha-1 chain is a protein that in humans is encoded by the TPM1 gene.[4]
This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy.[5]
Interactions
TPM1 has been shown to interact with TPM2.[6]
References
- ↑ compound #2d, Frédérick R, Dumont W, Ooms F, Aschenbach L, Van der Schyf CJ, Castagnoli N, Wouters J, Krief A (June 2006). "Synthesis, structural reassignment, and biological activity of type B MAO inhibitors based on the 5H-indeno[1,2-c]pyridazin-5-one core". J. Med. Chem. 49 (12): 3743–7. doi:10.1021/jm051091j. PMID 16759116.
- ↑ compound #2, Matos MJ, Vazquez-Rodriguez S, Uriarte E, Santana L, Viña D (July 2011). "MAO inhibitory activity modulation: 3-Phenylcoumarins versus 3-benzoylcoumarins". Bioorg. Med. Chem. Lett. 21 (14): 4224–7. doi:10.1016/j.bmcl.2011.05.074. PMID 21684743.
- ↑ compound #41, Catto M, Nicolotti O, Leonetti F, Carotti A, Favia AD, Soto-Otero R, Méndez-Alvarez E, Carotti A (2006). "Structural insights into monoamine oxidase inhibitory potency and selectivity of 7-substituted coumarins from ligand- and target-based approaches". Journal of Medicinal Chemistry 49 (16): 4912–25. doi:10.1021/jm060183l. PMID 16884303.
- ↑ Mogensen J, Kruse TA, Borglum AD (Jun 1999). "Refined localization of the human alpha-tropomyosin gene (TPM1) by genetic mapping". Cytogenet Cell Genet 84 (1-2): 35–6. doi:10.1159/000015207. PMID 10343096.
- ↑ "Entrez Gene: TPM1 tropomyosin 1 (alpha)".
- ↑ Brown, H R; Schachat F H (Apr 1985). "Renaturation of skeletal muscle tropomyosin: implications for in vivo assembly". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 82 (8): 2359–63. doi:10.1073/pnas.82.8.2359. ISSN 0027-8424. PMC 397557. PMID 3857586.
Further reading
- Lees-Miller JP, Helfman DM (1992). "The molecular basis for tropomyosin isoform diversity.". BioEssays 13 (9): 429–37. doi:10.1002/bies.950130902. PMID 1796905.
- Balvay L, Fiszman MY (1995). "[Analysis of the diversity of tropomyosin isoforms]". C. R. Seances Soc. Biol. Fil. 188 (5-6): 527–40. PMID 7780795.
- Gunning P, Weinberger R, Jeffrey P (1997). "Actin and tropomyosin isoforms in morphogenesis.". Anat. Embryol. 195 (4): 311–5. doi:10.1007/s004290050050. PMID 9108196.
- Perry SV (2002). "Vertebrate tropomyosin: distribution, properties and function.". J. Muscle Res. Cell. Motil. 22 (1): 5–49. doi:10.1023/A:1010303732441. PMID 11563548.
- Perry SV (2004). "What is the role of tropomyosin in the regulation of muscle contraction?". J. Muscle Res. Cell. Motil. 24 (8): 593–6. doi:10.1023/B:JURE.0000009811.95652.68. PMID 14870975.
- Jääskeläinen P, Miettinen R, Kärkkäinen P, et al. (2004). "Genetics of hypertrophic cardiomyopathy in eastern Finland: few founder mutations with benign or intermediary phenotypes.". Ann. Med. 36 (1): 23–32. doi:10.1080/07853890310017161. PMID 15000344.
- Mak A, Smillie LB, Bárány M (1978). "Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle.". Proc. Natl. Acad. Sci. U.S.A. 75 (8): 3588–92. doi:10.1073/pnas.75.8.3588. PMC 392830. PMID 278975.
- Höner B, Shoeman RL, Traub P (1992). "Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease.". Cell Biol. Int. Rep. 16 (7): 603–12. doi:10.1016/S0309-1651(06)80002-0. PMID 1516138.
- Chevray PM, Nathans D (1992). "Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun.". Proc. Natl. Acad. Sci. U.S.A. 89 (13): 5789–93. doi:10.1073/pnas.89.13.5789. PMC 402103. PMID 1631061.
- Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease.". FEBS Lett. 278 (2): 199–203. doi:10.1016/0014-5793(91)80116-K. PMID 1991513.
- Cho YJ, Liu J, Hitchcock-DeGregori SE (1990). "The amino terminus of muscle tropomyosin is a major determinant for function.". J. Biol. Chem. 265 (1): 538–45. PMID 2136742.
- Colote S, Widada JS, Ferraz C, et al. (1988). "Evolution of tropomyosin functional domains: differential splicing and genomic constraints.". J. Mol. Evol. 27 (3): 228–35. doi:10.1007/BF02100079. PMID 3138425.
- Lin CS, Leavitt J (1988). "Cloning and characterization of a cDNA encoding transformation-sensitive tropomyosin isoform 3 from tumorigenic human fibroblasts.". Mol. Cell. Biol. 8 (1): 160–8. PMC 363096. PMID 3336357.
- MacLeod AR, Gooding C (1988). "Human hTM alpha gene: expression in muscle and nonmuscle tissue.". Mol. Cell. Biol. 8 (1): 433–40. PMC 363144. PMID 3336363.
- Mische SM, Manjula BN, Fischetti VA (1987). "Relation of streptococcal M protein with human and rabbit tropomyosin: the complete amino acid sequence of human cardiac alpha tropomyosin, a highly conserved contractile protein.". Biochem. Biophys. Res. Commun. 142 (3): 813–8. doi:10.1016/0006-291X(87)91486-0. PMID 3548719.
- Heeley DH, Golosinska K, Smillie LB (1987). "The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C.". J. Biol. Chem. 262 (21): 9971–8. PMID 3611073.
- Brown HR, Schachat FH (1985). "Renaturation of skeletal muscle tropomyosin: implications for in vivo assembly.". Proc. Natl. Acad. Sci. U.S.A. 82 (8): 2359–63. doi:10.1073/pnas.82.8.2359. PMC 397557. PMID 3857586.
- Tanokura M, Ohtsuki I (1984). "Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I and troponin C.". J. Biochem. 95 (5): 1417–21. PMID 6746613.
- Pearlstone JR, Smillie LB (1983). "Effects of troponin-I plus-C on the binding of troponin-T and its fragments to alpha-tropomyosin. Ca2+ sensitivity and cooperativity.". J. Biol. Chem. 258 (4): 2534–42. PMID 6822572.
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