Difference between revisions of "Phosphatase Family OCA"
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Yeast OCA members are involved in cell cycle arrest in response to oxidative damage<cite>Alic</cite>, in telomere capping <cite>lydall08</cite>, in actin organization <cite>Care</cite>. [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>. | Yeast OCA members are involved in cell cycle arrest in response to oxidative damage<cite>Alic</cite>, in telomere capping <cite>lydall08</cite>, in actin organization <cite>Care</cite>. [[Gene_OCA3|OCA3]] has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase <cite>Harashima08</cite>. | ||
| − | + | === References === | |
<biblio> | <biblio> | ||
#Alic pmid=11408586 | #Alic pmid=11408586 | ||
Revision as of 23:55, 26 February 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: OCA
The OCA family is named after the five member genes in yeast (OCA1-5 = Oxidant-induced Cell-cycle Arrest). The family is also called plant and fungi atypical (PFA)-DSPs [1, 2].
Contents
Evolution
OCA is found in most eukaryotes other than eumetazoa. We have seen it in fungi, plants, protists, monosiga, and sponge.
Domain
OCA has a single domain, a phosphatase domain of fold CC1.
Functions
Yeast OCA members are involved in cell cycle arrest in response to oxidative damage[3], in telomere capping [4], in actin organization [5]. OCA3 has been shown to control intracellular localization of Gln3 (a phosphorylated transcriptional activator), in cooperation with Npr1 kinase [6].
References
- Romá-Mateo C, Ríos P, Tabernero L, Attwood TK, and Pulido R. A novel phosphatase family, structurally related to dual-specificity phosphatases, that displays unique amino acid sequence and substrate specificity. J Mol Biol. 2007 Dec 7;374(4):899-909. DOI:10.1016/j.jmb.2007.10.008 |
- Romá-Mateo C, Sacristán-Reviriego A, Beresford NJ, Caparrós-Martín JA, Culiáñez-Macià FA, Martín H, Molina M, Tabernero L, and Pulido R. Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms. Mol Genet Genomics. 2011 Apr;285(4):341-54. DOI:10.1007/s00438-011-0611-6 |
- Alic N, Higgins VJ, and Dawes IW. Identification of a Saccharomyces cerevisiae gene that is required for G1 arrest in response to the lipid oxidation product linoleic acid hydroperoxide. Mol Biol Cell. 2001 Jun;12(6):1801-10. DOI:10.1091/mbc.12.6.1801 |
- Addinall SG, Downey M, Yu M, Zubko MK, Dewar J, Leake A, Hallinan J, Shaw O, James K, Wilkinson DJ, Wipat A, Durocher D, and Lydall D. A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied cellular processes influencing telomere capping in Saccharomyces cerevisiae. Genetics. 2008 Dec;180(4):2251-66. DOI:10.1534/genetics.108.092577 |
- Care A, Vousden KA, Binley KM, Radcliffe P, Trevethick J, Mannazzu I, and Sudbery PE. A synthetic lethal screen identifies a role for the cortical actin patch/endocytosis complex in the response to nutrient deprivation in Saccharomyces cerevisiae. Genetics. 2004 Feb;166(2):707-19. DOI:10.1534/genetics.166.2.707 |
- Hirasaki M, Kaneko Y, and Harashima S. Protein phosphatase Siw14 controls intracellular localization of Gln3 in cooperation with Npr1 kinase in Saccharomyces cerevisiae. Gene. 2008 Feb 15;409(1-2):34-43. DOI:10.1016/j.gene.2007.11.005 |
