| First Author | Vogt L | Year | 2001 |
| Journal | Mol Cell Neurosci | Volume | 17 |
| Issue | 1 | Pages | 151-66 |
| PubMed ID | 11161476 | Mgi Jnum | J:67326 |
| Mgi Id | MGI:1930389 | Doi | 10.1006/mcne.2000.0937 |
| Citation | Vogt L, et al. (2001) Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain. Mol Cell Neurosci 17(1):151-66 |
| abstractText | 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. |
