Journal article
Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1
Molecular biology of the cell, Vol.13(2), pp.621-631
02/2002
DOI: 10.1091/mbc.01-11-0547
PMCID: PMC65654
PMID: 11854417
Abstract
Recent studies indicate that regulation of the actin cytoskeleton is important for protein trafficking, but its precise role is unclear. We have characterized the ARF1-dependent assembly of actin on the Golgi apparatus. Actin recruitment involves Cdc42/Rac and requires the activation of the Arp2/3 complex. Although the actin-binding proteins mAbp1 (SH3p7) and drebrin share sequence homology, they are differentially segregated into two distinct ARF-dependent actin complexes. The binding of Cdc42 and mAbp1, which localize to the Golgi apparatus, but not drebrin, is blocked by occupation of the p23 cargo-protein-binding site on coatomer. Exogenously expressed mAbp1 is mislocalized and inhibits Golgi transport in whole cells. The ability of ARF, vesicle-coat proteins, and cargo to direct the assembly of cytoskeletal structures helps explain how only a handful of vesicle types can mediate the numerous trafficking steps in the cell.
Details
- Title: Subtitle
- Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1
- Creators
- Raymond V Fucini - University of IowaJi-Long Chen - University of IowaCatherine Sharma - University of IowaMichael M Kessels - Department of Neurochemistry and Molecular Biology, Leibniz Institute of Neurobiology, Magdeburg D-39008, GermanyMark Stamnes - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Molecular biology of the cell, Vol.13(2), pp.621-631
- DOI
- 10.1091/mbc.01-11-0547
- PMID
- 11854417
- PMCID
- PMC65654
- ISSN
- 1059-1524
- eISSN
- 1939-4586
- Language
- English
- Date published
- 02/2002
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297608002771
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