Biology:FHL3
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Four and a half LIM domains protein 3 is a protein that in humans is encoded by the FHL3 gene.[1][2][3]
LIM proteins are defined by the possession of a highly conserved double zinc finger motif called the LIM domain.[3]
Function
FHL3 plays a role in myogenesis,[4] and also stimulates the development of neural crest by enhancing BMP signaling.[5]
Interactions
FHL3 has been shown to interact with:
References
- ↑ "Slim defines a novel family of LIM-proteins expressed in skeletal muscle". Biochem Biophys Res Commun 225 (2): 632–8. October 1996. doi:10.1006/bbrc.1996.1222. PMID 8753811.
- ↑ "Chromosomal mapping of a skeletal muscle specific LIM-only protein FHL3 to the distal end of the short arm of human chromosome 1". Somat Cell Mol Genet 24 (3): 197–202. May 1999. doi:10.1023/B:SCAM.0000007122.03392.4b. PMID 10226657.
- ↑ 3.0 3.1 "Entrez Gene: FHL3 four and a half LIM domains 3". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2275.
- ↑ Cottle et al., J Cell Sci. 2007 Apr 15;120(Pt 8):1423-35. doi: 10.1242/jcs.004739
- ↑ Intracellular enhancement of BMP signaling by LIM-domain protein FHL3 controls spatiotemporal emergence of the neural crest driven by WNT signaling Mansour Alkobtawi, Patrick Pla, Anne H. Monsoro-Burq bioRxiv 711192; doi: https://doi.org/10.1101/711192
- ↑ 6.0 6.1 "A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM". Mol. Cell. Biol. 20 (22): 8613–22. November 2000. doi:10.1128/mcb.20.22.8613-8622.2000. PMID 11046156.
- ↑ 7.0 7.1 "The LIM protein FHL3 binds basic Krüppel-like factor/Krüppel-like factor 3 and its co-repressor C-terminal-binding protein 2". J. Biol. Chem. 278 (15): 12786–95. April 2003. doi:10.1074/jbc.M300587200. PMID 12556451.
- ↑ "Protein–protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET)". J. Cell. Biochem. 80 (3): 293–303. 2001. doi:10.1002/1097-4644(20010301)80:3<293::AID-JCB10>3.0.CO;2-U. PMID 11135358.
- ↑ "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor". J. Biol. Chem. 279 (27): 28641–52. July 2004. doi:10.1074/jbc.M312894200. PMID 15117962.
Further reading
- "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle.". Biochem. Biophys. Res. Commun. 255 (2): 245–50. 1999. doi:10.1006/bbrc.1999.0179. PMID 10049693.
- "Protein–protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET).". J. Cell. Biochem. 80 (3): 293–303. 2001. doi:10.1002/1097-4644(20010301)80:3<293::AID-JCB10>3.0.CO;2-U. PMID 11135358.
- "The LIM protein FHL3 binds basic Krüppel-like factor/Krüppel-like factor 3 and its co-repressor C-terminal-binding protein 2.". J. Biol. Chem. 278 (15): 12786–95. 2003. doi:10.1074/jbc.M300587200. PMID 12556451.
- "LIM-only protein FHL3 interacts with CDC25B2 phosphatase.". Exp. Cell Res. 285 (1): 99–106. 2003. doi:10.1016/S0014-4827(03)00018-1. PMID 12681290.
- "FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly.". J. Biol. Chem. 278 (26): 24139–52. 2003. doi:10.1074/jbc.M213259200. PMID 12704194.
- "Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes.". Mol. Cell. Biol. 24 (3): 1081–95. 2004. doi:10.1128/MCB.24.3.1081-1095.2004. PMID 14729955.
- "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor.". J. Biol. Chem. 279 (27): 28641–52. 2004. doi:10.1074/jbc.M312894200. PMID 15117962.
- "FHL3 negatively regulates human high-affinity IgE receptor beta-chain gene expression by acting as a transcriptional co-repressor of MZF-1.". Biochem. J. 386 (Pt 1): 191–200. 2005. doi:10.1042/BJ20040775. PMID 15453830.
- "The SRF target gene Fhl2 antagonizes RhoA/MAL-dependent activation of SRF.". Mol. Cell 16 (6): 867–80. 2005. doi:10.1016/j.molcel.2004.11.039. PMID 15610731.
- "Towards a proteome-scale map of the human protein–protein interaction network.". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "FHL3 binds MyoD and negatively regulates myotube formation.". J. Cell Sci. 120 (Pt 8): 1423–35. 2007. doi:10.1242/jcs.004739. PMID 17389685.
External links
- FHL3+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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