Dual specificity protein phosphatase 2 is an enzyme that in humans is encoded by the DUSP2gene.[1][2][3][4]
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1 and ERK2, is predominantly expressed in hematopoietic tissues, and is localized in the nucleus.[4]
References
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↑Yi H, Morton CC, Weremowicz S, McBride OW, Kelly K (Dec 1995). "Genomic organization and chromosomal localization of the DUSP2 gene, encoding a MAP kinase phosphatase, to human 2p11.2-q11". Genomics. 28 (1): 92–6. doi:10.1006/geno.1995.1110. PMID7590752.
↑Yin Y, Liu YX, Jin YJ, Hall EJ, Barrett JC (Apr 2003). "PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression". Nature. 422 (6931): 527–31. doi:10.1038/nature01519. PMID12673251.
Wu J, Jin YJ, Calaf GM, et al. (2007). "PAC1 is a direct transcription target of E2F-1 in apoptotic signaling". Oncogene. 26 (45): 6526–35. doi:10.1038/sj.onc.1210484. PMID17471234.
Zhang Q, Muller M, Chen CH, et al. (2006). "New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding". J. Mol. Biol. 354 (4): 777–88. doi:10.1016/j.jmb.2005.10.006. PMID16288922.
Kothapalli R, Yoder SJ, Kusmartseva I, Loughran TP (2004). "Characterization of a variant of PAC-1 in large granular lymphocyte leukemia". Protein Expr. Purif. 32 (1): 52–60. doi:10.1016/S1046-5928(03)00237-7. PMID14680939.
Zhang Y, Guan DL, Xia CQ, et al. (2004). "Relationship between the expression levels of CD61, CD63, and PAC-1 on platelet surface in peripheral blood and the transplanted kidney function". Transplant. Proc. 35 (4): 1360–3. doi:10.1016/S0041-1345(03)00469-X. PMID12826159.
Farooq A, Plotnikova O, Chaturvedi G, et al. (2003). "Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP". Structure. 11 (2): 155–64. doi:10.1016/S0969-2126(02)00943-7. PMID12575935.
Ward Y, Gupta S, Jensen P, et al. (1994). "Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1". Nature. 367 (6464): 651–4. doi:10.1038/367651a0. PMID8107850.
Rohan PJ, Davis P, Moskaluk CA, et al. (1993). "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase". Science. 259 (5102): 1763–6. doi:10.1126/science.7681221. PMID7681221.
Raingeaud J, Gupta S, Rogers JS, et al. (1995). "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine". J. Biol. Chem. 270 (13): 7420–6. doi:10.1074/jbc.270.13.7420. PMID7535770.
