1. Vesicle endocytosis requires dynamin-dependent GTP hydrolysis at a fast CNS synapse
- Author
-
Takayuki Yamashita, Toshihide Hige, and Tomoyuki Takahashi
- Subjects
Botulinum Toxins ,Patch-Clamp Techniques ,GTP' ,Endocytic cycle ,Guanosine ,Biology ,In Vitro Techniques ,Endocytosis ,Electric Capacitance ,Guanosine Diphosphate ,Synaptic Transmission ,Exocytosis ,Bulk endocytosis ,chemistry.chemical_compound ,Animals ,Rats, Wistar ,Dynamin I ,Dynamin ,Multidisciplinary ,Hydrolysis ,Excitatory Postsynaptic Potentials ,Thionucleotides ,Peptide Fragments ,Rats ,chemistry ,Biochemistry ,Guanosine 5'-O-(3-Thiotriphosphate) ,Synapses ,Biophysics ,Calcium ,Guanosine Triphosphate ,Synaptic Vesicles ,Calyx of Held ,Brain Stem - Abstract
Molecular dependence of vesicular endocytosis was investigated with capacitance measurements at the calyx of Held terminal in brainstem slices. Intraterminal loading of botulinum toxin E revealed that the rapid capacitance transient implicated as “kiss-and-run” was unrelated to transmitter release. The release-related capacitance change decayed with an endocytotic time constant of 10 to 25 seconds, depending on the magnitude of exocytosis. Presynaptic loading of the nonhydrolyzable guanosine 5′-triphosphate (GTP) analog GTPgS or dynamin-1 proline-rich domain peptide abolished endocytosis. These compounds had no immediate effect on exocytosis, but caused a use-dependent rundown of exocytosis. Thus, the guanosine triphosphatase dynamin-1 is indispensable for vesicle endocytosis at this fast central nervous system (CNS) synapse.
- Published
- 2005