NDLI: Functional Regulation of Semaphorin Receptors by Proprotein Convertases

Content Provider	Journal of Biological Chemistry (JBC)
Author	Artigiani, Stefania Barberis, Davide Fazzari, Pietro Longati, Paola Angelini, Paola Loo, Jan-Willem Van De Comoglio, Paolo M. Tamagnone, Luca
Abstract	PLEXIN genes encode receptors for secreted and membrane-bound semaphorins. It was proposed that the extracellular domain of plexins acts as an inhibitory moiety, preventing receptor activation. Here we show that plexin-B1 and plexin-B2 undergo proteolytic processing in their extracellular portion, thereby converting single-chain precursors into non-disulfide-linked, heterodimeric receptors. We demonstrate that plexin processing is mediated by subtilisin-like proprotein convertases, by inhibition with α1-antitrypsin Portland, and by mutagenesis of the substrate-cleavage sites. We provide evidence indicating that proprotein convertases cleave plexins in a post-Golgi compartment and, likely, at the cell surface. In addition, we find that both cell surface targeting and proteolytic processing of plexin-B1 depend on protein-protein interaction motifs in the cytoplasmic domain of the receptor. We then show that proteolytic conversion of plexin-B1 into a heterodimeric receptor greatly increases the binding and the functional response to its specific ligand semaphorin 4D/CD100. Thus, we conclude that cleavage by proprotein convertases is a novel regulatory step for semaphorin receptors localized at the cell surface.
Related Links	http://www.jbc.org/content/278/12/10094.abstract
Ending Page	10101
Starting Page	10094
Page Count	8
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	12
Volume Number	278
DOI	10.1074/jbc.M210156200
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2003-03-21
Access Restriction	Open
Subject Keyword	Proprotein convertase (PC) Vesicular stomatitis virus (VSV) GlutathioneS-transferase (GST) Madin-Darby canine kidney cells (MDCK) Horseradish peroxidase (HRP) Nitro blue tetrazolium/5-bromo-4-chloro-3-indolyl phosphate (NBT/BCIP) PROTEIN SYNTHESIS POST-TRANSLATION MODIFICATION AND DEGRADATION
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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