title: Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain.
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.affiliation: Institute of Biochemistry, Institute of Anatomy, University of Zurich, Winterthurerstrasse 190, Zurich, CH-8057, Switzerland.
authors.forename: L
authors.initials: L
authors.lastname: Vogt
authors.forename: S P
authors.initials: SP
authors.lastname: Schrimpf
authors.forename: V
authors.initials: V
authors.lastname: Meskenaite
authors.forename: R
authors.initials: R
authors.lastname: Frischknecht
authors.forename: J
authors.initials: J
authors.lastname: Kinter
authors.forename: D P
authors.initials: DP
authors.lastname: Leone
authors.forename: U
authors.initials: U
authors.lastname: Ziegler
authors.forename: P
authors.initials: P
authors.lastname: Sonderegger
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D022081:Cell Surface Extensions / Q000378:metabolism; D002645:Chickens; D029721:Drosophila Proteins; D004331:Drosophila melanogaster; D005260:Female; D017403:In Situ Hybridization; D008297:Male; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009928:Organ Specificity; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D051381:Rats; D017208:Rats, Wistar; D017386:Sequence Homology, Amino Acid; D013570:Synaptic Membranes / Q000378:metabolism* / Q000648:ultrastructure; D013574:Synaptosomes / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; C503227:Clstn1 protein, mouse; D029721:Drosophila Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C503224:cals protein, Drosophila; C033652:postsynaptic density proteins; D002118:Calcium