Publication Date:
2001-09-05
Description:
The seven-subunit Arp2/3 complex choreographs the formation of branched actin networks at the leading edge of migrating cells. When activated by Wiskott-Aldrich Syndrome protein (WASp), the Arp2/3 complex initiates actin filament branches from the sides of existing filaments. Electron cryomicroscopy and three-dimensional reconstruction of Acanthamoeba castellanii and Saccharomyces cerevisiae Arp2/3 complexes bound to the WASp carboxy-terminal domain reveal asymmetric, oblate ellipsoids. Image analysis of actin branches indicates that the complex binds the side of the mother filament, and Arp2 and Arp3 (for actin-related protein) are the first two subunits of the daughter filament. Comparison to the actin-free, WASp-activated complexes suggests that branch initiation involves large-scale structural rearrangements within Arp2/3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkmann, N -- Amann, K J -- Stoilova-McPhie, S -- Egile, C -- Winter, D C -- Hazelwood, L -- Heuser, J E -- Li, R -- Pollard, T D -- Hanein, D -- New York, N.Y. -- Science. 2001 Sep 28;293(5539):2456-9. Epub 2001 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Burnham Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533442" target="_blank"〉PubMed〈/a〉
Keywords:
Acanthamoeba
;
Actin Cytoskeleton/*metabolism/ultrastructure
;
Actin-Related Protein 2
;
Actin-Related Protein 3
;
Actins/*chemistry/*metabolism
;
Animals
;
Cryoelectron Microscopy
;
*Cytoskeletal Proteins
;
Fourier Analysis
;
Image Processing, Computer-Assisted
;
Microscopy, Electron
;
Models, Molecular
;
Proteins/metabolism
;
Saccharomyces cerevisiae
;
Wiskott-Aldrich Syndrome Protein
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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