Biology:OCRL
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Inositol polyphosphate 5-phosphatase OCRL-1, also known as Lowe oculocerebrorenal syndrome protein, is an enzyme encoded by the OCRL gene located on the X chromosome in humans.[1]
This gene encodes an inositol polyphosphate 5-phosphatase. The responsible gene locus is at Xq26.1. This phosphatase enzyme is in part responsible for regulating membrane trafficking actin polymerization, and is located in several subcellular parts of the trans-Golgi network.
Deficiencies in OCRL-1 are associated with oculocerebrorenal syndrome[2] and also have been linked to Dent's disease.[3][4]
References
- ↑ "Entrez Gene: oculocerebrorenal syndrome of Lowe". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4952.
- ↑ "Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes". Am. J. Med. Genet. 77 (5): 348–55. June 1998. doi:10.1002/(SICI)1096-8628(19980605)77:5<348::AID-AJMG2>3.0.CO;2-J. PMID 9632163.
- ↑ Online Mendelian Inheritance in Man (OMIM) 300555
- ↑ "Dent Disease with mutations in OCRL1". Am. J. Hum. Genet. 76 (2): 260–7. February 2005. doi:10.1086/427887. PMID 15627218.
Further reading
- "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. 2005. doi:10.1038/nature03440. PMID 15772651. Bibcode: 2005Natur.434..325R.
- "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway.". Dev. Cell 13 (3): 377–90. 2007. doi:10.1016/j.devcel.2007.08.004. PMID 17765681.
- "Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases.". EMBO J. 25 (16): 3750–61. 2006. doi:10.1038/sj.emboj.7601274. PMID 16902405.
- "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.". EMBO J. 28 (13): 1831–42. 2009. doi:10.1038/emboj.2009.155. PMID 19536138.
- "Abnormal bradykinin signalling in fibroblasts deficient in the PIP(2) 5-phosphatase, ocrl1.". J. Inherit. Metab. Dis. 32 (2): 280–8. 2009. doi:10.1007/s10545-009-1058-3. PMID 19172411. https://zenodo.org/record/1232850.
- "Mutational analysis of CLC-5, cofilin and CLC-4 in patients with Dent's disease.". Nephron Physiol 112 (4): 53–62. 2009. doi:10.1159/000225944. PMID 19546591.
- "Lowe syndrome patient fibroblasts display Ocrl1-specific cell migration defects that cannot be rescued by the homologous Inpp5b phosphatase.". Hum. Mol. Genet. 18 (23): 4478–91. 2009. doi:10.1093/hmg/ddp407. PMID 19700499.
- "Locus heterogeneity of Dent's disease: OCRL1 and TMEM27 genes in patients with no CLCN5 mutations.". Pediatr. Nephrol. 24 (10): 1967–73. 2009. doi:10.1007/s00467-009-1228-4. PMID 19582483.
- "Lowe syndrome protein Ocrl1 is translocated to membrane ruffles upon Rac GTPase activation: a new perspective on Lowe syndrome pathophysiology.". Hum. Mol. Genet. 14 (11): 1441–8. 2005. doi:10.1093/hmg/ddi153. PMID 15829501.
- "OCRL1 mutations in Dent 2 patients suggest a mechanism for phenotypic variability.". Nephron Physiol 112 (2): 27–36. 2009. doi:10.1159/000213506. PMID 19390221.
- "OCRL1 mutations in patients with Dent disease phenotype in Japan.". Pediatr. Nephrol. 22 (7): 975–80. 2007. doi:10.1007/s00467-007-0454-x. PMID 17384968.
- "[Oculo-cerebro-renal Lowe syndrome: clinical, biochemical and molecular studies in a Moroccan patient]". Ann. Biol. Clin. (Paris) 64 (1): 53–9. 2006. PMID 16420990.
- "Lowe syndrome protein OCRL1 interacts with clathrin and regulates protein trafficking between endosomes and the trans-Golgi network.". Mol. Biol. Cell 16 (8): 3467–79. 2005. doi:10.1091/mbc.E05-02-0120. PMID 15917292.
- "Mutations in OCRL1 gene in Indian children with Lowe syndrome.". Clin. Exp. Nephrol. 12 (5): 358–62. 2008. doi:10.1007/s10157-008-0059-0. PMID 18500547.
- "OCRL1 function in renal epithelial membrane traffic.". Am. J. Physiol. Renal Physiol. 298 (2): F335-45. 2010. doi:10.1152/ajprenal.00453.2009. PMID 19940034.
- "All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding.". Biochem. Biophys. Res. Commun. 369 (2): 493–9. 2008. doi:10.1016/j.bbrc.2008.02.067. PMID 18307981. Bibcode: 2008BBRC..369..493M.
- "Dent Disease with mutations in OCRL1.". Am. J. Hum. Genet. 76 (2): 260–7. 2005. doi:10.1086/427887. PMID 15627218.
- "[From gene to disease; Dent's disease caused by abnormalities in the CLCN5 and OCRL1 genes]". Ned Tijdschr Geneeskd 151 (43): 2377–80. 2007. PMID 18019214.
- "Differential clathrin binding and subcellular localization of OCRL1 splice isoforms.". J. Biol. Chem. 284 (15): 9965–73. 2009. doi:10.1074/jbc.M807442200. PMID 19211563.
- "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1.". Proc. Natl. Acad. Sci. U.S.A. 107 (8): 3511–6. 2010. doi:10.1073/pnas.0914658107. PMID 20133602. Bibcode: 2010PNAS..107.3511S.
External links
- GeneReviews/NCBI/NIH/UW entry on Lowe Syndrome
- OCRL+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Inositol polyphosphate 5-phosphatase OCRL-1
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