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proteins. Page last changed on 19 Aug 2016.
Dual specificity phosphatase 18
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 dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP18 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009] (from
Sun et al., Beijing, China. In Spinal Cord, Nov 2015
Moreover, the TFs ZBTB7A and ELK1 and their target gene (dual specificity phosphatase 18 (DUSP18)) might be therapeutic targets for the treatment of SCI.Spinal Cord advance online publication, 27 October 2015; doi:10.1038/sc.2015.171.
Cesareni et al., Roma, Italy. In Front Genet, 2013
By this approach we rediscover several previously described phosphatase substrate interactions and characterize two new protein scaffolds that promote the dephosphorylation of PTPN11 and ERK by DUSP18 and DUSP26, respectively.