Disease relevance of DUSP7

• Relatively high levels of PYST2 were detected in a variety of myeloid leukemia and other cancer cell lines [1].

High impact information on DUSP7

• Inhibition of T cell antigen receptor signaling by VHR-related MKPX (VHX), a new dual specificity phosphatase related to VH1 related (VHR) [2].
• Expression VHR-related MKPX (VHX) was highest in thymus, but also detectable in monocytes and lymphocytes [2].
• Pyst2 binds p42 MAP kinase in vivo and both MAP kinase binding and substrate selectivity correlate with the ability of different recombinant MAP and SAP kinases to cause catalytic activation of the Pyst2 phosphatase in vitro [3].
• This reinforces the conclusion that Pyst1 and Pyst2 are members of a distinct and structurally homologous subfamily of dual-specificity (Thr/Tyr) MAP kinase phosphatases [3].
• We find that Pyst2 mRNA is constitutively expressed in a wide variety of human cell lines including those derived from ovarian, bladder and breast cancers [3].

Biological context of DUSP7

• Functional bioinformatic analysis of both transcripts revealed that exon 2 exists in only one of the PYST2 transcripts, designated PYST2-L, and has the consensus elements of the phosphatase catalytic domain (PCD) [4].
• A computer-based analysis of the PYST2 locus revealed that it harbors two alternative open reading frames promoted by two conserved promoter regions [4].

Anatomical context of DUSP7

• Pyst2 protein is predominantly cytosolic when expressed in COS-1 cells [3].
• While there is no evidence for inducible expression of Pyst2 mRNA in human skin fibroblasts in response to cellular stress, Pyst2 mRNA levels are moderately increased in response to serum stimulation [3].
• However, only two of these genes, the dual-specificity MAPK phosphatase PYST2 and the tryptophan 5-hydroxylase, were found to be more highly expressed by the leukemic-phase than by remission-phase leukocytes of all three patients [5].
• In the present study, high levels of PYST2 mRNA were detected by RT-PCR and by Northern blotting in bone marrow (BM) leukocytes and in peripheral blood mononuclear cells from additional eight AML patients [1].

Associations of DUSP7 with chemical compounds

• One of such genes was Phosphorylates tyrosine serine threonine 2 (PYST2), a dual-specificity Mitogen-activated protein (MAP) kinase (MAPK) phosphatase [1].

Other interactions of DUSP7

• Analysis of the predicted Pyst2-S protein revealed the presence of the vertebrate metallothionein signature I, the mammalian defensin, and the zinc-containing alcohol dehydrogenase motifs [4].

Analytical, diagnostic and therapeutic context of DUSP7

• The microarray results of only the PYST2 gene could be verified by RT-PCR [5].
• cDNA microarray analysis reveals an overexpression of the dual-specificity MAPK phosphatase PYST2 in acute leukemia [5].

References