FERMT3
Fermitin family homolog 3) (FERMT3), also known as kindlin-3 (KIND3), MIG2-like protein (MIG2B), or unc-112-related protein 2 (URP2) is a protein that in humans is encoded by the FERMT3 gene.[1][2][3]
Function
Kindlins are a small family of proteins that mediate protein-protein interactions involved in integrin activation and thereby have a role in cell adhesion, migration, differentiation, and proliferation. The FERMT3 protein has a key role in the regulation of hemostasis and thrombosis. This protein may also help maintain the membrane skeleton of erythrocytes.[1]
Clinical significance
Mutations in this gene cause the autosomal recessive leukocyte adhesion deficiency syndrome-III (LAD-III).[1]
References
- ^ a b c "Entrez Gene: fermitin family homolog 3 (Drosophila)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83706.
- ^ Weinstein EJ, Bourner M, Head R, Zakeri H, Bauer C, Mazzarella R (April 2003). "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas". Biochim. Biophys. Acta 1637 (3): 207–16. doi:10.1016/S0925-4439(03)00035-8. PMID 12697302.
- ^ Boyd RS, Adam PJ, Patel S, Loader JA, Berry J, Redpath NT, Poyser HR, Fletcher GC, Burgess NA, Stamps AC, Hudson L, Smith P, Griffiths M, Willis TG, Karran EL, Oscier DG, Catovsky D, Terrett JA, Dyer MJ (August 2003). "Proteomic analysis of the cell-surface membrane in chronic lymphocytic leukemia: identification of two novel proteins, BCNP1 and MIG2B". Leukemia 17 (8): 1605–12. doi:10.1038/sj.leu.2402993. PMID 12886250.
Further reading
- Etzioni A (2009). "Genetic etiologies of leukocyte adhesion defects.". Curr. Opin. Immunol. 21 (5): 481–6. doi:10.1016/j.coi.2009.07.005. PMID 19647987.
- Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442147.
- Bialkowska K, Ma YQ, Bledzka K, et al. (2010). "The integrin co-activator Kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell.". J. Biol. Chem. 285 (24): 18640–9. doi:10.1074/jbc.M109.085746. PMID 20378539.
- McDowall A, Svensson L, Stanley P, et al. (2010). "Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro.". Blood 115 (23): 4834–42. doi:10.1182/blood-2009-08-238709. PMID 20357244.
- Harburger DS, Bouaouina M, Calderwood DA (2009). "Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects.". J. Biol. Chem. 284 (17): 11485–97. doi:10.1074/jbc.M809233200. PMC 2670154. PMID 19240021. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2670154.
- Svensson L, Howarth K, McDowall A, et al. (2009). "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation.". Nat. Med. 15 (3): 306–12. doi:10.1038/nm.1931. PMID 19234463.
- Kuijpers TW, van de Vijver E, Weterman MA, et al. (2009). "LAD-1/variant syndrome is caused by mutations in FERMT3.". Blood 113 (19): 4740–6. doi:10.1182/blood-2008-10-182154. PMID 19064721.
- Mory A, Feigelson SW, Yarali N, et al. (2008). "Kindlin-3: a new gene involved in the pathogenesis of LAD-III.". Blood 112 (6): 2591. doi:10.1182/blood-2008-06-163162. PMID 18779414.
- Wang L, Deng W, Shi T, Ma D (2008). "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and apoptosis.". Biochem. Biophys. Res. Commun. 368 (4): 899–906. doi:10.1016/j.bbrc.2008.02.024. PMID 18280249.
- Manevich-Mendelson E, Feigelson SW, Pasvolsky R, et al. (2009). "Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions.". Blood 114 (11): 2344–53. doi:10.1182/blood-2009-04-218636. PMID 19617577.
- 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.
- 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.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
- Moser M, Bauer M, Schmid S, et al. (2009). "Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells.". Nat. Med. 15 (3): 300–5. doi:10.1038/nm.1921. PMID 19234461.
- Siegel DH, Ashton GH, Penagos HG, et al. (2003). "Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome.". Am. J. Hum. Genet. 73 (1): 174–87. doi:10.1086/376609. PMC 1180579. PMID 12789646. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1180579.
- Jurk K, Schulz AS, Kehrel BE, et al. (2010). "Novel integrin-dependent platelet malfunction in siblings with leukocyte adhesion deficiency-III (LAD-III) caused by a point mutation in FERMT3.". Thromb. Haemost. 103 (5): 1053–64. doi:10.1160/TH09-10-0689. PMID 20216991.
- Malinin NL, Zhang L, Choi J, et al. (2009). "A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans.". Nat. Med. 15 (3): 313–8. doi:10.1038/nm.1917. PMID 19234460.
- Lai-Cheong JE, Parsons M, McGrath JA (2010). "The role of kindlins in cell biology and relevance to human disease.". Int. J. Biochem. Cell Biol. 42 (5): 595–603. doi:10.1016/j.biocel.2009.10.015. PMID 19854292.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.