| Structural highlights
Function
PLPP_MOUSE Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP (By similarity).PGP_MOUSE Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism (PubMed:26755581). Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear (PubMed:24338473, PubMed:26755581). In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (PubMed:24338473).[1] [2]
Publication Abstract from PubMed
Mammalian haloacid dehalogenase (HAD)-type phosphatases are an emerging family of phosphatases with important functions in physiology and disease, yet little is known about the basis of their substrate specificity. Here, we characterize a previously unexplored HAD family member (gene annotation: phosphoglycolate phosphatase) that we termed AUM, for aspartate-based, ubiquitous, Mg2+-dependent phosphatase. AUM is a tyrosine-specific paralog of the serine/threonine-specific protein and pyridoxal 5'-phosphate-directed HAD phosphatase chronophin. Comparative evolutionary and biochemical analyses reveal that a single, differently conserved residue in the cap domain of either AUM or chronophin is crucial for phosphatase specificity. We have solved the X-ray crystal structure of the AUM cap fused to the catalytic core of chronophin to 2.65 A resolution and present a detailed view of the catalytic clefts of AUM and chronophin that explains their substrate preferences. Our findings identify a small number of cap domain residues that encode the different substrate specificities of AUM and chronophin.
Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities.,Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A J Biol Chem. 2013 Dec 13. PMID:24338473[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A. Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities. J Biol Chem. 2013 Dec 13. PMID:24338473 doi:http://dx.doi.org/10.1074/jbc.M113.503359
- ↑ Mugabo Y, Zhao S, Seifried A, Gezzar S, Al-Mass A, Zhang D, Lamontagne J, Attane C, Poursharifi P, Iglesias J, Joly E, Peyot ML, Gohla A, Madiraju SR, Prentki M. Identification of a mammalian glycerol-3-phosphate phosphatase: Role in metabolism and signaling in pancreatic beta-cells and hepatocytes. Proc Natl Acad Sci U S A. 2016 Jan 26;113(4):E430-9. doi: , 10.1073/pnas.1514375113. Epub 2016 Jan 11. PMID:26755581 doi:http://dx.doi.org/10.1073/pnas.1514375113
- ↑ Seifried A, Knobloch G, Duraphe PS, Segerer G, Manhard J, Schindelin H, Schultz J, Gohla A. Evolutionary and Structural Analyses of the Mammalian Haloacid Dehalogenase-Type Phosphatases AUM and Chronophin Provide Insight into the Basis of their Different Substrate Specificities. J Biol Chem. 2013 Dec 13. PMID:24338473 doi:http://dx.doi.org/10.1074/jbc.M113.503359
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