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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Calcium / metabolism*
-
Calcium-Binding Proteins / genetics
-
Calcium-Binding Proteins / metabolism*
-
Cell Surface Extensions / metabolism
-
Chickens
-
Drosophila Proteins
-
Drosophila melanogaster
-
Female
-
In Situ Hybridization
-
Male
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism*
-
Mice
-
Mice, Inbred C57BL
-
Molecular Sequence Data
-
Nerve Tissue Proteins / metabolism
-
Organ Specificity
-
Protein Processing, Post-Translational*
-
Protein Structure, Tertiary
-
Rats
-
Rats, Wistar
-
Sequence Homology, Amino Acid
-
Synaptic Membranes / metabolism*
-
Synaptic Membranes / ultrastructure
-
Synaptosomes / metabolism
Substances
-
Calcium-Binding Proteins
-
Clstn1 protein, mouse
-
Drosophila Proteins
-
Membrane Proteins
-
Nerve Tissue Proteins
-
cals protein, Drosophila
-
postsynaptic density proteins
-
Calcium
Associated data
-
GENBANK/AJ289016
-
GENBANK/AJ289017
-
GENBANK/AJ289018