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Atypical DUSPs: 19 phosphatases in search of a role

AuthorsBayón, Yolanda ; Alonso, Andrés
Issue Date2010
PublisherTransworld Research Network (Trivandrum, India)
CitationEmerging Signaling Pathways in Tumor Biology: 185-208 (2010)
AbstractAtypical Dual Specificity Phosphatases (A-DUSPs) are a group of 19 phosphatases poorly characterized. They are included among the Class I Cys-based PTPs and contain the active site motif HCXXGXXR conserved in the Class I PTPs. These enzymes present a phosphatase domain similar to MKPs, but lack any substrate targeting domain similar to the CH2 present in this group. Although most of these phosphatases have no more than 250 amino acids, their size ranges from the 150 residues of the smallest A-DUSP, VHZ/DUSP23, to the 1158 residues of the putative PTP DUSP27. The substrates of this family include MAPK, but, in general terms, it does not look that MAPK are the general substrates for the whole group. In fact, other substrates have been described for some of these phosphatases, like the 5’CAP structure of mRNA, glycogen, or STATs and still the substrates of many A-DUSPs have not been identified. In addition to the PTP domain, most of these enzymes present no additional recognizable domains in their sequence, with the exception of CBM-20 in laforin, GTase in HCE1 and a Zn binding domain in DUSP12. Although some of these enzymes have been now studied for years there is a great lack of data about the true physiological role of this group of phosphatases.
Description24 páginas, 1 figura, 1 tabla.
Publisher version (URL)http://www.trnres.com/ebookcontents.php?id=72
Appears in Collections:(IBGM) Libros y partes de libros
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