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Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain.

Authors: Vogt, L  Schrimpf, S P  Meskenaite, V  Frischknecht, R  Kinter, J  Leone, D P  Ziegler, U  Sonderegger, P 
Citation: Vogt L, etal., Mol Cell Neurosci. 2001 Jan;17(1):151-66. doi: 10.1006/mcne.2000.0937.
Pubmed: (View Article at PubMed) PMID:11161476
DOI: Full-text: DOI:10.1006/mcne.2000.0937

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.


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CRRD Object Information
CRRD ID: 13702439
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.