Brain-specific Angiogenesis Inhibitor-1 Signaling, Regulation, and Enrichment in the Postsynaptic Density

• Type of Material: Article
• Authors: Jason R. Stephenson, Emory University; Kevin J. Paavola, Emory University; Stacy A. Schaefer, Emory University; Balveen Kaur, Emory University; Erwin Van Meir, Emory University; Randy A Hall, Emory University
• Language: English
• Date: 2013-08-02
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://dx.doi.org/10.1074/jbc.M113.489757
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 288
• Issue: 31
• Start Page: 22248
• End Page: 22256
• Grant/Funding Information: This work was supported in part by National Institutes of Health Grants NS072394 (to R. A. H.) and CA086335 and CA163722 (to E. G. V. M.).
• Keywords: BAI1; FAMILY; Biochemistry & Molecular Biology; SCAFFOLD; Life Sciences & Biomedicine; BETA-ARRESTINS; ADHESION-GPCRS; EMERGING ROLES; Science & Technology; ENGULFMENT RECEPTOR; APOPTOTIC CELLS; PROTEIN-COUPLED RECEPTORS; GENE
• Research Categories: Biology, Cell; Health Sciences, Medicine and Surgery

Abstract

Background: BAI1 is an adhesion receptor; little is known about its signaling or localization. Results: BAI1 activates Rho in a G protein-dependent manner, binds to synaptic scaffold proteins, and is highly enriched in the postsynaptic density. Conclusion: BAI1 is a synaptic receptor that signals through G proteins. Significance: BAI1 may play a previously unappreciated role as a regulator of synaptic function.