Abstract
The dual specificity phosphatases (DUSPs) are a subfamily within the protein tyrosine phosphatase (PTP) family, with the unique property of being able to hydrolyze phosphoserine or phospho-threonine residues and phospho-tyrosine residues [1]. All DUSPs share the characteristic Class I PTP consensus sequence, D...HC(X)5RS/T, with C representing the essential catalytic cysteine [1]. Unlike other PTPs, DUSPs lack the phospho-tyrosine recognition domain, resulting in a shallower catalytic cleft, most likely enabling DUSPs to dephosphorylate all three residues (S/T/Y) [1]. In addition to protein substrates, the DUSP subfamily contains members that dephosphorylate additional substrates including lipids, nucleic acids, and sugars [2].
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