Tropomodulin-3 is a protein that in humans is encoded by the TMOD3 gene.[5][6]
Tropomodulin-3 (Tmod3) is a member of the tropomodulin family of actin-regulatory proteins that plays a key role in modulating the dynamics of the cytoskeleton by capping the pointed (minus) ends of actin filaments. Unlike some other tropomodulin isoforms, Tmod3 is widely expressed in non-muscle cells, where it contributes to essential cellular processes such as shape maintenance, motility, and adhesion. It regulates filament stability by preventing both polymerization and depolymerization at the pointed end, thus helping to define actin filament length and organization.[7] In endothelial cells, Tmod3 has been shown to inhibit cell motility through its capping activity, highlighting its role as a negative regulator of actin-driven migration.[8] Additionally, Tmod3 can bind not only to filamentous actin but also directly to actin monomers, suggesting a broader function in actin filament turnover and cytoskeletal remodeling.[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000138594 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058587 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Cox PR, Zoghbi HY (Apr 2000). "Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs". Genomics. 63 (1): 97–107. doi:10.1006/geno.1999.6061. PMID 10662549.
- ^ "Entrez Gene: TMOD3 tropomodulin 3 (ubiquitous)".
- ^ a b Fischer RS, Yarmola EG, Weber KL, Speicher KD, Speicher DW, Bubb MR, et al. (2006-11-24). "Tropomodulin 3 Binds to Actin Monomers". The Journal of Biological Chemistry. 281 (47): 36454–36465. doi:10.1074/jbc.M606315200. ISSN 0021-9258. PMID 17012745.
- ^ Fischer RS, Fritz-Six KL, Fowler VM (April 2003). "Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility". The Journal of Cell Biology. 161 (2): 371–380. doi:10.1083/jcb.200209057. PMC 2172920. PMID 12707310.
Further reading
- Weber KL, Fischer RS, Fowler VM (Oct 2007). "Tmod3 regulates polarized epithelial cell morphology". Journal of Cell Science. 120 (Pt 20): 3625–3632. doi:10.1242/jcs.011445. PMID 17928307.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, et al. (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Fischer RS, Yarmola EG, Weber KL, Speicher KD, Speicher DW, Bubb MR, et al. (Nov 2006). "Tropomodulin 3 binds to actin monomers". Journal of Biological Chemistry. 281 (47): 36454–36465. doi:10.1074/jbc.M606315200. PMID 17012745.
- Pawlak G, McGarvey TW, Nguyen TB, Tomaszewski JE, Puthiyaveettil R, Malkowicz SB, et al. (Jun 2004). "Alterations in tropomyosin isoform expression in human transitional cell carcinoma of the urinary bladder". International Journal of Cancer. 110 (3): 368–373. doi:10.1002/ijc.20151. PMID 15095301. S2CID 875146.
- Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (Feb 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
- Fischer RS, Fritz-Six KL, Fowler VM (Apr 2003). "Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility". The Journal of Cell Biology. 161 (2): 371–380. doi:10.1083/jcb.200209057. PMC 2172920. PMID 12707310.
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See also: cytoskeletal defects |