The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin

Weidong Xu; Mark Stamnes

doi:10.1074/jbc.M510141200

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The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin

Journal article

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The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin

Weidong Xu and Mark Stamnes

The Journal of biological chemistry, Vol.281(17), pp.11826-11833

04/28/2006

DOI: 10.1074/jbc.M510141200

PMID: 16452483

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Abstract

Cytoskeletal dynamics are important for efficient function of the secretory pathway. ADP-ribosylation factor, ARF1, triggers vesicle coat assembly and, in concert with Cdc42, regulates actin polymerization and molecular motor-based motility. Drebrin and mammalian Abp1 (mAbp1) are actin-binding proteins found previously to bind to Golgi membranes in an ARF1-dependent manner in vitro. Despite sharing homology through two shared actin binding domains, drebrin and mAbp1 have different subcellular localization and bind to distinct actin structures on the Golgi apparatus. We find that the actin-depolymerizing factor homology (ADFH) and charged/helical actin binding domains of drebrin and mAbp1 are sufficient for regulated binding to Golgi membranes and subcellular localization. We have used mutant proteins and chimeras between mAbp1 and drebrin to identify motifs that direct targeting. We find that a linker region between the ADFH and charged/helical domains confers Golgi binding properties to mAbp1. mAbp1 binds to a specific actin pool through its ADFH/linker domain that is not bound by drebrin. Drebrin localization to the cell surface was found to involve motifs within the charged/helical domain. Our results indicate that targeting of these proteins is directed through multiple distinct interactions with the actin cytoskeleton. The mechanisms for selective recruitment of mAbp1 and drebrin to Golgi membranes indicate how actin-based structures are able to select specific actin-binding proteins and, thus, carry out multiple different functions within cells.

Protein Structure, Tertiary

Actins - metabolism

Rats

Neuropeptides - metabolism

Actin Depolymerizing Factors - metabolism

Golgi Apparatus

Animals

Cattle

Protein Binding

Cell Membrane - metabolism

Microfilament Proteins - metabolism

Neuropeptides - genetics

Subcellular Fractions

Microfilament Proteins - genetics

Actin Depolymerizing Factors - chemistry

Details

Title: Subtitle: The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin
Creators: Weidong Xu - Department of Physiology and Biophysics, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242, USA
Mark Stamnes
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.281(17), pp.11826-11833
DOI: 10.1074/jbc.M510141200
PMID: 16452483
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: GM068674 / NIGMS NIH HHS
Language: English
Date published: 04/28/2006
Academic Unit: Molecular Physiology and Biophysics; Internal Medicine
Record Identifier: 9984025345502771

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