Abstract：
:NCAM 180 isoform null neuromuscular junctions are unable to effectively mobilize and exocytose synaptic vesicles and thus exhibit periods of total transmission failure during high-frequency repetitive stimulation. We have identified a highly conserved C-terminal (KENESKA) domain on NCAM that is required to maintain effective transmission and demonstrate that it acts via a pathway involving MLCK and probably myosin light chain (MLC) and myosin II. By perfecting a method of introducing peptides into adult NMJs, we tested the hypothesized role of proteins in this pathway by competitive disruption of protein-protein interactions. The effects of KENESKA and other peptides on MLCK and MLC activation and on failures in both wild-type and NCAM 180 null junctions supported this pathway, and serine phosphorylation of KENESKA was critical. We propose that this pathway is required to replenish synaptic vesicles utilized during high levels of exocytosis by facilitating myosin-driven delivery of synaptic vesicles to active zones or their subsequent exocytosis.
journal_name
Neuronjournal_title
Neuronauthors
Polo-Parada L,Plattner F,Bose C,Landmesser LTdoi
10.1016/j.neuron.2005.05.018subject
Has Abstractpub_date
2005-06-16 00:00:00pages
917-31issue
6eissn
0896-6273issn
1097-4199pii
S0896-6273(05)00439-3journal_volume
46pub_type
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