Difference between revisions of "Phosphatase Subfamily STYX"
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| + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_STYX|Subfamily STYX]] | ||
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| + | STYX is a catalytically inactive phosphatase found in most opisthokonts but lost in nematodes. | ||
| + | |||
| + | === Evolution === | ||
| + | STYX is found in most opisthokonts but lost in nematodes. Although STYX is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi ([http://resdev.gene.com/gOrtholog/view/cluster/MC0005385/overview unpublished data from gOrtholog]). | ||
| + | |||
| + | === Domain === | ||
| + | STYX has a single domain, (inactive) phosphatase domain. | ||
| + | |||
| + | === Function === | ||
| + | STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. It binds to phosphorylated tyrosine to module signaling <cite>Wishart98</cite>. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>. STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>. | ||
| + | |||
| + | === References === | ||
| + | <biblio> | ||
| + | #Reiterer13 pmid=23847209 | ||
| + | #Wishart95 pmid=7592916 | ||
| + | #Wishart98 pmid=9757831 | ||
| + | #Wishart02 pmid=11842224 | ||
| + | </biblio> | ||
Latest revision as of 00:55, 2 October 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily STYX
STYX is a catalytically inactive phosphatase found in most opisthokonts but lost in nematodes.
Evolution
STYX is found in most opisthokonts but lost in nematodes. Although STYX is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi (unpublished data from gOrtholog).
Domain
STYX has a single domain, (inactive) phosphatase domain.
Function
STYX is catalytically inactive (pseudophosphatase) [1]. It binds to phosphorylated tyrosine to module signaling [2]. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export [3]. STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis [4].
References
- Wishart MJ, Denu JM, Williams JA, and Dixon JE. A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J Biol Chem. 1995 Nov 10;270(45):26782-5. DOI:10.1074/jbc.270.45.26782 |
- Wishart MJ and Dixon JE. Gathering STYX: phosphatase-like form predicts functions for unique protein-interaction domains. Trends Biochem Sci. 1998 Aug;23(8):301-6. DOI:10.1016/s0968-0004(98)01241-9 |
- Reiterer V, Fey D, Kolch W, Kholodenko BN, and Farhan H. Pseudophosphatase STYX modulates cell-fate decisions and cell migration by spatiotemporal regulation of ERK1/2. Proc Natl Acad Sci U S A. 2013 Jul 30;110(31):E2934-43. DOI:10.1073/pnas.1301985110 |
- Wishart MJ and Dixon JE. The archetype STYX/dead-phosphatase complexes with a spermatid mRNA-binding protein and is essential for normal sperm production. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2112-7. DOI:10.1073/pnas.251686198 |
