{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Grosshans BL"],"funding":["NCRR NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["55-66"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2063532"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["172(1)"],"pubmed_abstract":["Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation."],"journal":["The Journal of cell biology"],"pubmed_title":["The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p."],"pmcid":["PMC2063532"],"funding_grant_id":["P41 RR11823-10","GM 35370","R01 GM035370","R37 GM035370","P01 CA046128","CA 46128","R01GM54712","R01 GM054712","P41 RR011823"],"pubmed_authors":["Grosshans BL","Brennwald P","Yates JR","Niessen S","Gangar A","Novick P","Andreeva A"],"additional_accession":[]},"is_claimable":false,"name":"The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p.","description":"Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation.","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jan","modification":"2020-10-29T17:12:51Z","creation":"2019-03-26T23:02:21Z"},"accession":"S-EPMC2063532","cross_references":{"pubmed":["16390997"],"doi":["10.1083/jcb.200510016"]}}