Brain-specific angiogenesis inhibitor-1 signaling, regulation, and enrichment in the postsynaptic density

Jason R. Stephenson; Kevin J. Paavola; Stacy A. Schaefer; Balveen Kaur; Erwin G. Van Meir; Randy A. Hall

doi:10.1074/jbc.M113.489757

Brain-specific angiogenesis inhibitor-1 signaling, regulation, and enrichment in the postsynaptic density

Jason R. Stephenson, Kevin J. Paavola, Stacy A. Schaefer, Balveen Kaur, Erwin G. Van Meir, Randy A. Hall

Research output: Contribution to journal › Article › peer-review

82 Scopus citations

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.

Original language	English (US)
Pages (from-to)	22248-22256
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	288
Issue number	31
DOIs	https://doi.org/10.1074/jbc.M113.489757
State	Published - Aug 2 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.489757

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title = "Brain-specific angiogenesis inhibitor-1 signaling, regulation, and enrichment in the postsynaptic density",

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.",

author = "Stephenson, {Jason R.} and Paavola, {Kevin J.} and Schaefer, {Stacy A.} and Balveen Kaur and {Van Meir}, {Erwin G.} and Hall, {Randy A.}",

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AU - Stephenson, Jason R.

AU - Paavola, Kevin J.

AU - Schaefer, Stacy A.

AU - Kaur, Balveen

AU - Van Meir, Erwin G.

AU - Hall, Randy A.

PY - 2013/8/2

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N2 - 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.

AB - 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.

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Brain-specific angiogenesis inhibitor-1 signaling, regulation, and enrichment in the postsynaptic density

Abstract

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