Dual specificity phosphatase

spinqualitylabelsall models Human Cdc14B2 core domain (cyan) complex with tripeptide (green) and acetyl (PDB code 1ohe). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Dual specificity phosphatase or Dual specificity protein phosphatase (DUSP) is a phosphatase which dephosphorylates phosphotyrosine, phosphoserine or phosphothreonine residues. There are several DUSP enzymes in mammals sharing a common catalytic mechanism. The DUSP include: • Slingshot phosphatase • Phosphatase of regenerating liver (PRL) • Cdc14 leads to mitotic exit by dephosphorylation of targets of the protein kinase Cdk1. • Cdc25 activates Cdk1 by its dephosphorylation. • PTEN (Phosphatase and TEnsin homolog) dephosphorylates phosphasitide substrates. For details see PTEN. • Myotubularin dephosphorylates phosphadinylinositol 3-phosphate and phosphadinylinositol (3,5)-bi-phosphate • MAPK phosphatase see MAP kinase phosphatase Relevance Cdc25A and Cdc25B are overexpressed in several types of cancers and their inhibitors are being tested as chemotherapeutic agents. PTEN gene is mutated with high frequency in a variety of human cancers. Phosphatase of regenerating liver is overexpressed in several types of cancers. Disease Myotubularin mutations are responsible for the hereditary motor disease Charcot-Marie-Tooth disease. Structural highlights Tripeptide binding site in human Cdc14B2 (PDB code 1ohe). 3D structures of dual specificity phosphatase Dual specificity phosphatase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman