Evidence for CALM in Directing VAMP2 Trafficking

Asaff Harel, Fangbai Wu, Mark P. Mattson, Christa M. Morris, Pamela J. Yao

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)417-429
Number of pages13
JournalTraffic
Volume9
Issue number3
DOIs
StatePublished - Mar 2008
Externally publishedYes

Keywords

  • Clathrin
  • Endocytosis
  • Flow cytometry
  • SiRNA
  • SNARE proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Structural Biology
  • Molecular Biology
  • Genetics

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