Document Detail

New insights into the regulation and cellular functions of the ARP2/3 complex.
MedLine Citation:
PMID:  23212475     Owner:  NLM     Status:  Publisher    
The actin-related protein 2/3 (ARP2/3) complex nucleates branched actin filament networks, but requires nucleation promoting factors (NPFs) to stimulate this activity. NPFs include proteins such as Wiskott-Aldrich syndrome protein (WASP), neural WASP (NWASP), WASP family verprolin-homologous protein (WAVE; also known as SCAR) and the recently identified WASP and SCAR homologue (WASH) complex. The mechanisms underlying NPF-dependent regulation and the cellular functions of ARP2/3 are being unravelled using new chemical and genetic approaches. Of particular interest is the role of the ARP2/3 complex in vesicular trafficking and directional cell motility.
Jeremy D Rotty; Congying Wu; James E Bear
Related Documents :
18485275 - Label-free optical detection of aptamer-protein interactions using gold-capped oxide na...
24162925 - Quantifying protein interaction dynamics by swath mass spectrometry: application to the...
24675275 - Molecular mechanisms enhancing the proteome of influenza a viruses: an overview of rece...
23436005 - Why does a protein's evolutionary rate vary over time?
7894675 - Enhanced albumin protein separations and protein-drug binding constant measurements usi...
11406615 - The brain exocyst complex interacts with rala in a gtp-dependent manner: identification...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-05
Journal Detail:
Title:  Nature reviews. Molecular cell biology     Volume:  -     ISSN:  1471-0080     ISO Abbreviation:  Nat. Rev. Mol. Cell Biol.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100962782     Medline TA:  Nat Rev Mol Cell Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
UNC Lineberger Comprehensive Cancer Center, Department of Cell Biology and Physiology, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA; and at the Howard Hughes Medical Institute.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Diet and dental topography in pitheciine seed predators.
Next Document:  The nuclear lamins: flexibility in function.