{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Purcell RH"],"funding":["National Institute of Neurological Disorders and Stroke","NIH Office of the Director","NINDS NIH HHS","National Human Genome Research Institute"],"pagination":["1751-1760"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5679302"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["38(12)"],"pubmed_abstract":["Mutations in G protein-coupled receptors (GPCRs) that increase constitutive signaling activity can cause human disease. A de novo C-terminal mutation (R1465W) in the adhesion GPCR BAI2 (also known as ADGRB2) was identified in a patient suffering from progressive spastic paraparesis and other neurological symptoms. In vitro studies revealed that this mutation strongly increases the constitutive signaling activity of an N-terminally cleaved form of BAI2, which represents the activated form of the receptor. Further studies dissecting the mechanism(s) underling this effect revealed that wild-type BAI2 primarily couples to Gα<sub>z</sub> , with the R1465W mutation conferring increased coupling to Gα<sub>i</sub> . The R1465W mutation also increases the total and surface expression of BAI2. The m"],"journal":["Human mutation"],"pubmed_title":["A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases receptor signaling activity."],"pmcid":["PMC5679302"],"funding_grant_id":["T32 NS096050","R21 NS094136).","R21 NS094136"],"pubmed_authors":["Purcell RH","Toro C","Gahl WA","Hall RA"],"additional_accession":[]},"is_claimable":false,"name":"A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases receptor signaling activity.","description":"Mutations in G protein-coupled receptors (GPCRs) that increase constitutive signaling activity can cause human disease. A de novo C-terminal mutation (R1465W) in the adhesion GPCR BAI2 (also known as ADGRB2) was identified in a patient suffering from progressive spastic paraparesis and other neurological symptoms. In vitro studies revealed that this mutation strongly increases the constitutive signaling activity of an N-terminally cleaved form of BAI2, which represents the activated form of the receptor. Further studies dissecting the mechanism(s) underling this effect revealed that wild-type BAI2 primarily couples to Gα<sub>z</sub> , with the R1465W mutation conferring increased coupling to Gα<sub>i</sub> . The R1465W mutation also increases the total and surface expression of BAI2. The m","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Dec","modification":"2025-04-22T09:11:05.395Z","creation":"2019-03-27T00:09:08Z"},"accession":"S-EPMC5679302","cross_references":{"pubmed":["28891236"],"doi":["10.1002/humu.23336"]}}