FBLIM1
Filamin-binding LIM protein 1 is a protein that in humans is encoded by the FBLIM1 gene.[1][2][3]
This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.[3]
Interactions
FBLIM1 has been shown to interact with Filamin,[1] PLEKHC1[1] and FLNB.[2]
References
Further reading
- Wu C (2005). "Migfilin and its binding partners: from cell biology to human diseases". J. Cell. Sci. 118 (Pt 4): 659–64. doi:10.1242/jcs.01639. PMID 15701922.
- 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Akazawa H, Kudoh S, Mochizuki N et al. (2004). "A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5". J. Cell Biol. 164 (3): 395–405. doi:10.1083/jcb.200309159. PMC 2172236. PMID 14757752. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172236.
- Brandenberger R, Wei H, Zhang S et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
- 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Gkretsi V, Zhang Y, Tu Y et al. (2005). "Physical and functional association of migfilin with cell-cell adhesions". J. Cell. Sci. 118 (Pt 4): 697–710. doi:10.1242/jcs.01638. PMID 15671069.
- 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.
- Oh JH, Yang JO, Hahn Y et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
- Zhang Y, Tu Y, Gkretsi V, Wu C (2006). "Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration". J. Biol. Chem. 281 (18): 12397–407. doi:10.1074/jbc.M512107200. PMID 16531412.
- Gregory SG, Barlow KF, McLay KE et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
- Papachristou DJ, Gkretsi V, Tu Y et al. (2007). "Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma". Histopathology 51 (4): 499–508. doi:10.1111/j.1365-2559.2007.02791.x. PMC 2768333. PMID 17711449. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2768333.