Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to de-phosphorylate both tyrosine (EC22.214.171.124) and serine / threonine (EC126.96.36.199) residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK, JNK, and p38 with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminalCdc25-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses.
It is known to bind and dephosphorylate ErkII, and as it, along with the other members of the DUSP family expresses high selectively for MAP kinases, it has been suggested that it functions as a method for selectively activating/deactivating different members of that family.
^Muda M, Boschert U, Dickinson R, Martinou JC, Martinou I, Camps M, Schlegel W, Arkinstall S (Jun 1996). "MKP-3, a novel cytosolic protein-tyrosine phosphatase that exemplifies a new class of mitogen-activated protein kinase phosphatase". J Biol Chem271 (8): 4319–26. doi:10.1074/jbc.271.8.4319. PMID8626780.
^Smith A, Price C, Cullen M, Muda M, King A, Ozanne B, Arkinstall S, Ashworth A (Sep 1997). "Chromosomal localization of three human dual specificity phosphatase genes (DUSP4, DUSP6, and DUSP7)". Genomics42 (3): 524–7. doi:10.1006/geno.1997.4756. PMID9205128.
^Patterson KI, Brummer T, O'Brien PM, Daly RJ (March 2009). "Dual-specificity phosphatases: critical regulators with diverse cellular targets". Biochem. J.418 (3): 475–89. PMID19228121.
^Dowd S, Sneddon AA, Keyse SM (November 1998). "Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases". J. Cell. Sci.111 (22): 3389–99. PMID9788880.
Dowd S, Sneddon AA, Keyse SM (1999). "Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases". J. Cell. Sci.111 (22): 3389–99. PMID9788880.
Pasquali C, Curchod ML, Wälchli S et al. (2004). "Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor". Mol. Endocrinol.17 (11): 2228–39. doi:10.1210/me.2003-0011. PMID12907755.
Levy-Nissenbaum O, Sagi-Assif O, Kapon D et al. (2003). "Dual-specificity phosphatase Pyst2-L is constitutively highly expressed in myeloid leukemia and other malignant cells". Oncogene22 (48): 7649–60. doi:10.1038/sj.onc.1206971. PMID14576828.
Levy-Nissenbaum O, Sagi-Assif O, Witz IP (2004). "Characterization of the dual-specificity phosphatase PYST2 and its transcripts". Genes Chromosomes Cancer39 (1): 37–47. doi:10.1002/gcc.10295. PMID14603440.
Orlev LN, Ehud B, Tamar BG et al. (2004). "Does the dual-specificity MAPK phosphatase Pyst2-L lead a monogamous relationship with the Erk2 protein?". Immunol. Lett.92 (1–2): 149–56. doi:10.1016/j.imlet.2003.11.024. PMID15081539.