Journal Article

PUBDB-2015-01331

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A Conformational Switch in Collybistin Determines the Differentiation of Inhibitory Postsynapses

Soykan, T. ; Schneeberger, D.>Extern* ; Tria, G.>Extern*EMBL* ; Buechner, C. ; Bader, N. ; Svergun, D.>Extern*EMBL* ; Tessmer, I. ; Poulopoulos, A. ; Papadopoulos, T. ; Varoqueaux, F. ; Schindelin, H. (Corresponding author) ; Brose, N. (Corresponding author)

2014
EMBO Press Heidelberg

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Please use a persistent id in citations: doi:10.15252/embj.201488143

Abstract: The formation of neuronal synapses and the dynamic regulation of their efficacy depend on the assembly of the postsynaptic neurotransmitter receptor apparatus. Receptor recruitment to inhibitory GABAergic and glycinergic synapses is controlled by the scaffold protein gephyrin and the adaptor protein collybistin. We derived new insights into the structure of collybistin and used these to design biochemical, cell biological, and genetic analyses of collybistin function. Our data define a collybistin‐based protein interaction network that controls the gephyrin content of inhibitory postsynapses. Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides. This function of collybistin is regulated by binding of the adhesion protein neuroligin‐2, which stabilizes the open/active conformation of collybistin at the postsynaptic plasma membrane by competing with an intramolecular interaction in collybistin that favors the closed/inactive conformation. By linking trans‐synaptic neuroligin‐dependent adhesion and phosphoinositide signaling with gephyrin recruitment, the collybistin‐based regulatory switch mechanism represents an integrating regulatory node in the formation and function of inhibitory postsynapses.

Note: (c) The Authors

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Contributing Institute(s):

1. EMBL (EMBL)
2. EMBL-User (EMBL-User)

Research Program(s):

1. DORIS Beamline D1.2 (POF2-54G13) (POF2-54G13)
2. EUROSPIN - European Consortium on Synaptic Protein Networks in Neurological and Psychiatric Diseases (241498) (241498)
3. SYNSYS - Synaptic Systems: dissecting brain function in health and disease (242167) (242167)
4. BIOSTRUCT-X - Transnational access and enhancement of integrated Biological Structure determination at synchrotron X-ray radiation facilities (283570) (283570)

Experiment(s):

1. DORIS Beamline D1.2 (DORIS III)

Appears in the scientific report 2014

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Database coverage:
; ; BIOSIS Previews ; Current Contents - Life Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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