Evidence for CALM in Directing VAMP2 Trafficking
Open Access
- 21 December 2007
- Vol. 9 (3), 417-429
- https://doi.org/10.1111/j.1600-0854.2007.00694.x
Abstract
Clathrin assembly lymphoid myeloid leukemia protein (CALM) is a clathrin assembly protein with a domain structure similar to the neuron‐specific assembly protein AP180. We have previously found that CALM is expressed in neurons and present in synapses. We now report that CALM has a neuron‐related function: it facilitates the endocytosis of the synaptic vesicle protein VAMP2 from the plasma membrane. Overexpression of CALM leads to the reduction of cell surface VAMP2, whereas knockdown of CALM by RNA interference results in the accumulation of surface VAMP2. The AP180 N‐terminal homology (ANTH) domain of CALM is required for its effect on VAMP2 trafficking, and the ANTH domain itself acts as a dominant‐negative mutant. Thus, our results reveal a role for CALM in directing VAMP2 trafficking during endocytosis.Keywords
This publication has 45 references indexed in Scilit:
- Factors regulating the abundance and localization of synaptobrevin in the plasma membraneProceedings of the National Academy of Sciences, 2006
- The synaptic vesicle: cycle of exocytosis and endocytosisCurrent Opinion in Neurobiology, 2006
- Imaging of receptor trafficking by using α-bungarotoxin-binding-site-tagged receptorsProceedings of the National Academy of Sciences, 2004
- Specific Interaction between SNAREs and Epsin N-terminal Homology (ENTH) Domains of Epsin-related Proteins in trans-Golgi Network to Endosome TransportJournal of Biological Chemistry, 2004
- SNARE function revisitedNature Structural & Molecular Biology, 2003
- Membrane FusionCell, 2003
- Clathrin-binding proteins: Got a motif? Join the network!Trends in Cell Biology, 2001
- Simultaneous Binding of PtdIns(4,5)P 2 and Clathrin by AP180 in the Nucleation of Clathrin Lattices on MembranesScience, 2001
- Endocytosis of VAMP is facilitated by a synaptic vesicle targeting signal.The Journal of cell biology, 1996
- Bacterially expressed F1‐20/AP‐3 assembles clathrin into cages with a narrow size distribution: Implications for the regulation of quantal size during neurotransmissionJournal of Neuroscience Research, 1995