Evidence for CALM in Directing VAMP2 Trafficking

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

doi:10.1111/j.1600-0854.2007.00694.x

Evidence for CALM in Directing VAMP2 Trafficking

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

Research output: Contribution to journal › Article › peer-review

119 Scopus citations

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 language	English (US)
Pages (from-to)	417-429
Number of pages	13
Journal	Traffic
Volume	9
Issue number	3
DOIs	https://doi.org/10.1111/j.1600-0854.2007.00694.x
State	Published - Mar 2008
Externally published	Yes

Keywords

Clathrin
Endocytosis
Flow cytometry
SiRNA
SNARE proteins

ASJC Scopus subject areas

Biochemistry
Cell Biology
Structural Biology
Molecular Biology
Genetics

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10.1111/j.1600-0854.2007.00694.x

Cite this

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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.",

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AU - Harel, Asaff

AU - Wu, Fangbai

AU - Mattson, Mark P.

AU - Morris, Christa M.

AU - Yao, Pamela J.

PY - 2008/3

Y1 - 2008/3

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AB - 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.

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KW - Flow cytometry

KW - SiRNA

KW - SNARE proteins

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Evidence for CALM in Directing VAMP2 Trafficking

Abstract

Keywords

ASJC Scopus subject areas

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