TY - JOUR
T1 - The synaptic vesicle protein SV2 is complexed with an α5-containing laminin on the nerve terminal surface
AU - Son, Young Jin
AU - Scranton, Todd W.
AU - Sunderland, William J.
AU - Baek, Sung J.
AU - Miner, Jeffrey H.
AU - Sanes, Joshua R.
AU - Carlson, Steven S.
PY - 2000/1/7
Y1 - 2000/1/7
N2 - Interactions between growing axons and synaptic basal lamina components direct the formation of neuromuscular junctions during nerve regeneration. Isoforms of laminin containing α5 or β2 chains are potential basal lamina ligands for these interactions. The nerve terminal receptors are unknown. Here we show that SV2, a synaptic vesicle transmembrane proteoglycan, is complexed with a 900-kDa laminin on synaptosomes from the electric organ synapse that is similar to the neuromuscular junctions. Although two laminins are present on synaptosomes, only the 900-kDa laminin is associated with SV2. Other nerve terminal components are absent from this complex. The 900-kDa laminin contains an α5, a β1, and a novel γ chain. To test whether SV2 directly binds the 900-kDa laminin, we looked for interaction between purified SV2 and laminin-1, a laminin isoform with a similar structure. We find SV2 binds with high affinity to purified laminin-1. Our results suggest that a synaptic vesicle component may act as a laminin receptor on the presynaptic plasma membrane; they also suggest a mechanism for activity- dependent adhesion at the synapse.
AB - Interactions between growing axons and synaptic basal lamina components direct the formation of neuromuscular junctions during nerve regeneration. Isoforms of laminin containing α5 or β2 chains are potential basal lamina ligands for these interactions. The nerve terminal receptors are unknown. Here we show that SV2, a synaptic vesicle transmembrane proteoglycan, is complexed with a 900-kDa laminin on synaptosomes from the electric organ synapse that is similar to the neuromuscular junctions. Although two laminins are present on synaptosomes, only the 900-kDa laminin is associated with SV2. Other nerve terminal components are absent from this complex. The 900-kDa laminin contains an α5, a β1, and a novel γ chain. To test whether SV2 directly binds the 900-kDa laminin, we looked for interaction between purified SV2 and laminin-1, a laminin isoform with a similar structure. We find SV2 binds with high affinity to purified laminin-1. Our results suggest that a synaptic vesicle component may act as a laminin receptor on the presynaptic plasma membrane; they also suggest a mechanism for activity- dependent adhesion at the synapse.
UR - http://www.scopus.com/inward/record.url?scp=0034614456&partnerID=8YFLogxK
U2 - 10.1074/jbc.275.1.451
DO - 10.1074/jbc.275.1.451
M3 - Article
C2 - 10617638
AN - SCOPUS:0034614456
SN - 0021-9258
VL - 275
SP - 451
EP - 460
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 1
ER -