{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chinthalapudi K"],"funding":["NINDS NIH HHS"],"pagination":["1338"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5889391"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["Neurofibromatosis type 2 (NF2) is a tumor-forming disease of the nervous system caused by deletion or by loss-of-function mutations in NF2, encoding the tumor suppressing protein neurofibromin 2 (also known as schwannomin or merlin). Neurofibromin 2 is a member of the ezrin, radixin, moesin (ERM) family of proteins regulating the cytoskeleton and cell signaling. The correlation of the tumor-suppressive function and conformation (open or closed) of neurofibromin 2 has been subject to much speculation, often based on extrapolation from other ERM proteins, and controversy. Here we show that lipid binding results in the open conformation of neurofibromin 2 and that lipid binding is necessary for inhibiting cell proliferation. Collectively, our results provide a mechanism in which the open conf"],"journal":["Nature communications"],"pubmed_title":["Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2."],"pmcid":["PMC5889391"],"funding_grant_id":["R01 NS077952"],"pubmed_authors":["Zheng J","Kissil J","Mandati V","Izard T","Chinthalapudi K","Bricogne G","Sharff AJ","Griffin PR"],"additional_accession":[]},"is_claimable":false,"name":"Lipid binding promotes the open conformation and tumor-suppressive activity of neurofibromin 2.","description":"Neurofibromatosis type 2 (NF2) is a tumor-forming disease of the nervous system caused by deletion or by loss-of-function mutations in NF2, encoding the tumor suppressing protein neurofibromin 2 (also known as schwannomin or merlin). Neurofibromin 2 is a member of the ezrin, radixin, moesin (ERM) family of proteins regulating the cytoskeleton and cell signaling. The correlation of the tumor-suppressive function and conformation (open or closed) of neurofibromin 2 has been subject to much speculation, often based on extrapolation from other ERM proteins, and controversy. Here we show that lipid binding results in the open conformation of neurofibromin 2 and that lipid binding is necessary for inhibiting cell proliferation. Collectively, our results provide a mechanism in which the open conf","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2026-05-03T07:55:27.9Z","creation":"2019-03-26T23:28:01Z"},"accession":"S-EPMC5889391","cross_references":{"pubmed":["29626191"],"doi":["10.1038/s41467-018-03648-4"]}}