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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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 > Institute of Biochemistry|
07 Faculty of Science > Institute of Biochemistry
|DDC:||570 Life sciences; biology|
|Uncontrolled Keywords:||Neuron, Adhesion molecules, Cell-substratum distance, Extracellular electrodes|
|Date:||01 January 2001|
|Deposited On:||11 Feb 2008 13:20|
|Last Modified:||28 Nov 2013 00:54|
|Funders:||Swiss National Science foundation, SPP Biotechnology|
|Citations:||Web of Science®. Times cited: 40|
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