Home Publications Research Data Research Grants Inventions & Patents Awards Additional Research Activities Faculties & Institutions Research Areas

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

Vogt L, Schrimpf SP, Meskenaite V, Frischknecht R, Kinter J, Leone DP, Ziegler U, Sonderegger P (2001)

---

Publication Type: Journal article

Publication year: 2001

Journal

Book Volume: 17

Pages Range: 151-166

Journal Issue: 1

DOI: 10.1006/mcne.2000.0937

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.

Authors with CRIS profile

Involved external institutions

How to cite

APA:

Vogt, L., Schrimpf, S.P., Meskenaite, V., Frischknecht, R., Kinter, J., Leone, D.P.,... 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. https://doi.org/10.1006/mcne.2000.0937

MLA:

Vogt, Lorenz, et al. "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain." Molecular and Cellular Neuroscience 17.1 (2001): 151-166.

BibTeX: Download