Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Development ; 134(5): 967-77, 2007 Mar.
Article in English | MEDLINE | ID: mdl-17267444

ABSTRACT

The actin-nucleating ARP2-ARP3 complex controls cell shape in plants in many different cell types. Its activity is controlled by a multimeric complex containing BRK1 (also known as HSPC300), NAP1, SRA1, ABI and SCAR/WAVE. In this study, we focus on the function of the five putative SCAR homologues in Arabidopsis and we provide biochemical evidence that AtSCAR2 can activate the ARP2-ARP3 complex in vitro. Among the single mutants, mutations in only AtSCAR2 result in a subtle or weak phenotype similar to ARP2, ARP3 and other ;distorted' mutants. Double-mutant analysis revealed a redundancy with AtSCAR4. Systematic application of the yeast two-hybrid system and Bimolecular Fluorescence Complementation (BiFC) revealed a complex protein-interaction network between the ARP2-ARP3 complex and its genetically defined regulators. In addition to protein interactions known in other systems, we identified several new interactions, suggesting that SPIKE1 may be an integral component of the SCAR/WAVE complex and that SCAR proteins in plants might act as direct effectors of ROP GTPases.


Subject(s)
Actin-Related Protein 2-3 Complex/metabolism , Arabidopsis Proteins/physiology , Arabidopsis/physiology , Wiskott-Aldrich Syndrome Protein Family/physiology , Actin-Related Protein 2-3 Complex/genetics , Adenosine Triphosphatases/metabolism , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Cell Cycle Proteins/metabolism , Morphogenesis , Mutation , Protein Binding , Protein Interaction Mapping , Wiskott-Aldrich Syndrome Protein Family/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...