Oculocerebrorenal syndrome of Lowe

PDB rendering based on 2qv2.
External IDs OMIM300535 MGI109589 HomoloGene233 GeneCards: OCRL Gene
EC number
Species Human Mouse
Entrez 4952 320634
Ensembl ENSG00000122126 ENSMUSG00000001173
UniProt Q01968 Q6NVF0
RefSeq (mRNA) NM_000276.3 NM_177215.3
RefSeq (protein) NP_000267.2 NP_796189.2
Location (UCSC) Chr X:
128.67 – 128.73 Mb
Chr X:
45.27 – 45.32 Mb
PubMed search [1] [2]

Inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein is an enzyme that in humans is encoded by the OCRL gene located on the X chromosome.[1]

This gene encodes a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network.[1]


Clinical significance

Mutation in this gene are associated with oculocerebrorenal syndrome[2] and also with Dent's disease.[3][4]


  1. ^ a b "Entrez Gene: oculocerebrorenal syndrome of Lowe". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4952. 
  2. ^ Kawano T, Indo Y, Nakazato H, Shimadzu M, Matsuda I (June 1998). "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. doi:10.1002/(SICI)1096-8628(19980605)77:5<348::AID-AJMG2>3.0.CO;2-J. PMID 9632163. 
  3. ^ Online 'Mendelian Inheritance in Man' (OMIM) 300555
  4. ^ Hoopes RR, Shrimpton AE, Knohl SJ, et al. (February 2005). "Dent Disease with mutations in OCRL1". Am. J. Hum. Genet. 76 (2): 260–7. doi:10.1086/427887. PMC 1196371. PMID 15627218. http://linkinghub.elsevier.com/retrieve/pii/S0002-9297(07)62577-4. 

Further reading

  • Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMC 2665286. PMID 15772651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2665286. 
  • Erdmann KS, Mao Y, McCrea HJ, et al. (2007). "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway.". Dev. Cell 13 (3): 377–90. doi:10.1016/j.devcel.2007.08.004. PMID 17765681. 
  • Hyvola N, Diao A, McKenzie E, et al. (2006). "Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases.". EMBO J. 25 (16): 3750–61. doi:10.1038/sj.emboj.7601274. PMID 16902405. 
  • Mao Y, Balkin DM, Zoncu R, et al. (2009). "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.". EMBO J. 28 (13): 1831–42. doi:10.1038/emboj.2009.155. PMID 19536138. 
  • Suchy SF, Cronin JC, Nussbaum RL (2009). "Abnormal bradykinin signalling in fibroblasts deficient in the PIP(2) 5-phosphatase, ocrl1.". J. Inherit. Metab. Dis. 32 (2): 280–8. doi:10.1007/s10545-009-1058-3. PMID 19172411. 
  • Wu F, Reed AA, Williams SE, et al. (2009). "Mutational analysis of CLC-5, cofilin and CLC-4 in patients with Dent's disease.". Nephron Physiol 112 (4): p53-62. doi:10.1159/000225944. PMID 19546591. 
  • Coon BG, Mukherjee D, Hanna CB, et al. (2009). "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. doi:10.1093/hmg/ddp407. PMID 19700499. 
  • Tosetto E, Addis M, Caridi G, et al. (2009). "Locus heterogeneity of Dent's disease: OCRL1 and TMEM27 genes in patients with no CLCN5 mutations.". Pediatr. Nephrol. 24 (10): 1967–73. doi:10.1007/s00467-009-1228-4. PMID 19582483. 
  • Faucherre A, Desbois P, Nagano F, et al. (2005). "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. doi:10.1093/hmg/ddi153. PMID 15829501. 
  • Shrimpton AE, Hoopes RR, Knohl SJ, et al. (2009). "OCRL1 mutations in Dent 2 patients suggest a mechanism for phenotypic variability.". Nephron Physiol 112 (2): p27-36. doi:10.1159/000213506. PMID 19390221. 
  • Sekine T, Nozu K, Iyengar R, et al. (2007). "OCRL1 mutations in patients with Dent disease phenotype in Japan.". Pediatr. Nephrol. 22 (7): 975–80. doi:10.1007/s00467-007-0454-x. PMID 17384968. 
  • Chabaâ L, Monnier N, Dahri S, et al.. "[Oculo-cerebro-renal Lowe syndrome: clinical, biochemical and molecular studies in a Moroccan patient]". Ann. Biol. Clin. (Paris) 64 (1): 53–9. PMID 16420990. 
  • Choudhury R, Diao A, Zhang F, et al. (2005). "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. doi:10.1091/mbc.E05-02-0120. PMID 15917292. 
  • Sethi SK, Bagga A, Gulati A, et al. (2008). "Mutations in OCRL1 gene in Indian children with Lowe syndrome.". Clin. Exp. Nephrol. 12 (5): 358–62. doi:10.1007/s10157-008-0059-0. PMID 18500547. 
  • Cui S, Guerriero CJ, Szalinski CM, et al. (2010). "OCRL1 function in renal epithelial membrane traffic.". Am. J. Physiol. Renal Physiol. 298 (2): F335-45. doi:10.1152/ajprenal.00453.2009. PMID 19940034. 
  • McCrea HJ, Paradise S, Tomasini L, et al. (2008). "All known patient mutations in the ASH-RhoGAP domains of OCRL affect targeting and APPL1 binding.". Biochem. Biophys. Res. Commun. 369 (2): 493–9. doi:10.1016/j.bbrc.2008.02.067. PMID 18307981. 
  • Hoopes RR, Shrimpton AE, Knohl SJ, et al. (2005). "Dent Disease with mutations in OCRL1.". Am. J. Hum. Genet. 76 (2): 260–7. doi:10.1086/427887. PMC 1196371. PMID 15627218. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1196371. 
  • Levtchenko EN, Monnens LA, Bökenkamp A, Knoers NV (2007). "[From gene to disease; Dent's disease caused by abnormalities in the CLCN5 and OCRL1 genes]". Ned Tijdschr Geneeskd 151 (43): 2377–80. PMID 18019214. 
  • Choudhury R, Noakes CJ, McKenzie E, et al. (2009). "Differential clathrin binding and subcellular localization of OCRL1 splice isoforms.". J. Biol. Chem. 284 (15): 9965–73. doi:10.1074/jbc.M807442200. PMID 19211563. 
  • Swan LE, Tomasini L, Pirruccello M, et al. (2010). "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. doi:10.1073/pnas.0914658107. PMID 20133602. 

External links

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