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The Journal of Neuroscience, December 12, 2007, 27(50):13691-13700; doi:10.1523/JNEUROSCI.3910-07.2007

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Cellular/Molecular
Synaptic Vesicle Mobility in Mouse Motor Nerve Terminals with and without Synapsin

Michael A. Gaffield¹ and William J. Betz²

¹Neuroscience Program and ²Department of Physiology and Biophysics, University of Colorado Medical School, Anschutz Medical Campus, Aurora, Colorado 80045

Correspondence should be addressed to William J. Betz, Department of Physiology and Biophysics, University of Colorado Medical School, Anschutz Medical Campus, P.O. Box 6511, Mail Shop F8307, Aurora, CO 80045. Email: bill.betz{at}uchsc.edu

We measured synaptic vesicle mobility using fluorescence recovery after photobleaching of FM 1-43 [N-(3-triethylammoniumpropyl)-4-(4-(dibutylamino)styryl) pyridinium dibromide] stained mouse motor nerve terminals obtained from wild-type (WT) and synapsin triple knock-out (TKO) mice at room temperature and physiological temperature. Vesicles were mobile in resting terminals at physiological temperature but virtually immobile at room temperature. Mobility was increased at both temperatures by blocking phosphatases with okadaic acid, decreased at physiological temperature by blocking kinases with staurosporine, and unaffected by disrupting actin filaments with latrunculin A or reducing intracellular calcium concentration with BAPTA-AM. Synapsin TKO mice showed reduced numbers of synaptic vesicles and reduced FM 1-43 staining intensity. Synaptic transmission, however, was indistinguishable from WT, as was synaptic vesicle mobility under all conditions tested. Thus, in TKO mice, and perhaps WT mice, a phospho-protein different from synapsin but otherwise of unknown identity is the primary regulator of synaptic vesicle mobility.

Key words: synapsin; FRAP; temperature; synaptic vesicle mobility; motor nerve terminal; actin

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Received Aug. 27, 2007; revised Oct. 1, 2007; accepted Oct. 17, 2007.

Correspondence should be addressed to William J. Betz, Department of Physiology and Biophysics, University of Colorado Medical School, Anschutz Medical Campus, P.O. Box 6511, Mail Shop F8307, Aurora, CO 80045. Email: bill.betz{at}uchsc.edu

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