Journal article
Proteolysis of SNARE proteins alters facilitation and depression in a specific way
Proceedings of the National Academy of Sciences - PNAS, Vol.102(7), pp.2614-2619
02/15/2005
DOI: 10.1073/pnas.0409656102
PMCID: PMC549003
PMID: 15695333
Abstract
The molecular mechanisms of short-term plasticity observed during synaptic transmission are unknown. To determine whether the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a role in short-term plasticity, Botulinum toxins A, E, and F, were used to disrupt SNARE protein function in cultured hippocampal neurons. Although low concentrations of all of the toxins significantly reduced evoked release, they differentially affected short-term plasticity as assessed by the paired-pulse ratio, regardless of the initial release probability and size of the readily releasable pool of the synapse. The toxin effects on the paired-pulse ratio resulted in different phenotypes dependent on the toxin cleavage site. Together, these data indicate proteolysis of SNARE proteins alters facilitation and depression in a specific way.
Details
- Title: Subtitle
- Proteolysis of SNARE proteins alters facilitation and depression in a specific way
- Creators
- Samuel M Young Jr - Molecular Neurobiology Laboratory and Howard Hughes Medical Institute, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. syoung@gwdg.de
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.102(7), pp.2614-2619
- DOI
- 10.1073/pnas.0409656102
- PMID
- 15695333
- PMCID
- PMC549003
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Publisher
- National Academy of Sciences; United States
- Language
- English
- Date published
- 02/15/2005
- Academic Unit
- Anatomy and Cell Biology; Iowa Neuroscience Institute; Otolaryngology
- Record Identifier
- 9984025376102771
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