{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hodakoski C"],"funding":["NCATS NIH HHS","NIDDK NIH HHS","NCI NIH HHS","NIGMS NIH HHS","Biotechnology and Biological Sciences Research Council"],"pagination":["155-60"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3890808"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["111(1)"],"pubmed_abstract":["Insulin activation of phosphoinositide 3-kinase (PI3K) signaling regulates glucose homeostasis through the production of phosphatidylinositol 3,4,5-trisphosphate (PIP3). The dual-specificity phosphatase and tensin homolog deleted on chromosome 10 (PTEN) blocks PI3K signaling by dephosphorylating PIP3, and is inhibited through its interaction with phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 (P-REX2). The mechanism of inhibition and its physiological significance are not known. Here, we report that P-REX2 interacts with PTEN via two interfaces. The pleckstrin homology (PH) domain of P-REX2 inhibits PTEN by interacting with the catalytic region of PTEN, and the inositol polyphosphate 4-phosphatase domain of P-REX2 provides high-affinity binding to the postsynaptic densi"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Regulation of PTEN inhibition by the pleckstrin homology domain of P-REX2 during insulin signaling and glucose homeostasis."],"pmcid":["PMC3890808"],"funding_grant_id":["T32 CA009503","GM008224-20","R01 CA155117","UL1 TR000117","S06 GM008224","T32 CA009503-22","R01 DK71349","BBS/E/B/000C0415","R01 CA082783","R01 DK071349","BBS/E/B/000C0413"],"pubmed_authors":["Hopkins BD","Mense SM","Keniry M","Anderson KE","Barrows D","Parsons R","Stephens LR","Kern PA","Hodakoski C","Hawkins PT"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of PTEN inhibition by the pleckstrin homology domain of P-REX2 during insulin signaling and glucose homeostasis.","description":"Insulin activation of phosphoinositide 3-kinase (PI3K) signaling regulates glucose homeostasis through the production of phosphatidylinositol 3,4,5-trisphosphate (PIP3). The dual-specificity phosphatase and tensin homolog deleted on chromosome 10 (PTEN) blocks PI3K signaling by dephosphorylating PIP3, and is inhibited through its interaction with phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 (P-REX2). The mechanism of inhibition and its physiological significance are not known. Here, we report that P-REX2 interacts with PTEN via two interfaces. The pleckstrin homology (PH) domain of P-REX2 inhibits PTEN by interacting with the catalytic region of PTEN, and the inositol polyphosphate 4-phosphatase domain of P-REX2 provides high-affinity binding to the postsynaptic densi","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jan","modification":"2026-04-15T11:16:07.865Z","creation":"2026-04-07T13:56:01.626Z"},"accession":"S-EPMC3890808","cross_references":{"pubmed":["24367090"],"doi":["10.1073/pnas.1213773111"]}}