Journal
JOURNAL OF NEUROSCIENCE
Volume 33, Issue 26, Pages 10634-10646Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.0329-13.2013
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Funding
- NIMH
- Staglin Family/International Mental Health Research Organization
- Brain and Behavior Research Foundation (NARSAD)
- UCSF Program for Breakthrough Biomedical Research, Dean's Office, and Resource Allocation Program
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Increasing evidence indicates that individual synaptic vesicle proteins may use different signals, endocytic adaptors, and trafficking pathways for sorting to distinct pools of synaptic vesicles. Here, we report the identification of a unique amino acid motif in the vesicular GABA transporter (VGAT) that controls its synaptic localization and activity-dependent recycling. Mutational analysis of this atypical dileucine-like motif in rat VGAT indicates that the transporter recycles by interacting with the clathrin adaptor protein AP-2. However, mutation of a single acidic residue upstream of the dileucine-like motif leads to a shift to an AP-3-dependent trafficking pathway that preferentially targets the transporter to the readily releasable and recycling pool of vesicles. Real-time imaging with a VGAT-pHluorin fusion provides a useful approach to explore how unique sorting sequences target individual proteins to synaptic vesicles with distinct functional properties.
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