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Vogt, L; Schrimpf, S P; Meskenaite, V; Frischknecht, R; Kinter, J; Leone, D P; Ziegler, U; Sonderegger, P (2001). Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain. Molecular and Cellular Neuroscience, 17(1):151-166.

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Abstract

In a screen for proteins released from synapse-forming spinal cord neurons, we found the proteolytically cleaved N-terminal fragment of a transmembrane protein localized in the postsynaptic membrane of both excitatory and inhibitory synapses. We termed this protein calsyntenin-1, because it binds synaptic Ca2+ with its cytoplasmic domain. By binding Ca2+, calsyntenin-1 may modulate Ca2+-mediated postsynaptic signals. Proteolytic cleavage of calsyntenin-1 in its extracellular moiety generates a transmembrane stump that is internalized and accumulated in the spine apparatus of spine synapses. Therefore, the synaptic Ca2+ modulation by calsyntenin-1 may be subject to regulation by extracellular proteolysis in the synaptic cleft. Thus, calsyntenin-1 may link extracellular proteolysis in the synaptic cleft and postsynaptic Ca2+ signaling.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
DDC:570 Life sciences; biology
Uncontrolled Keywords:Neuron, Adhesion molecules, Cell-substratum distance, Extracellular electrodes
Language:English
Date:1 January 2001
Deposited On:11 Feb 2008 12:20
Last Modified:27 Nov 2013 23:54
Publisher:Elsevier
ISSN:1044-7431
Funders:Swiss National Science foundation, SPP Biotechnology
Publisher DOI:10.1006/mcne.2000.0937
PubMed ID:11161476
Citations:Web of Science®. Times Cited: 44
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