BRICK1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabidopsis
Autor: | Stevan Djakovic, Michael Burke, Mary J. Frank, Laurie G. Smith, Julia Dyachok |
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Rok vydání: | 2006 |
Předmět: |
Talin
Multiprotein complex Mutant Molecular Sequence Data Morphogenesis Arabidopsis Arp2/3 complex macromolecular substances Cell morphology Actin-Related Protein 2-3 Complex Plant Epidermis Gene Expression Regulation Plant Amino Acid Sequence Cytoskeleton Molecular Biology Cell Shape Actin Conserved Sequence biology Arabidopsis Proteins Microfilament Proteins biology.organism_classification Plants Genetically Modified Actins Cell biology Mutation biology.protein Microscopy Electron Scanning Sequence Alignment Developmental Biology Protein Binding |
Zdroj: | Development (Cambridge, England). 133(6) |
ISSN: | 0950-1991 |
Popis: | The Arp2/3 complex, a highly conserved nucleator of F-actin polymerization,is essential for a variety of eukaryotic cellular processes, including epidermal cell morphogenesis in Arabidopsis thaliana. Efficient nucleation of actin filaments by the Arp2/3 complex requires the presence of an activator such as a member of the Scar/WAVE family. In mammalian cells, a multiprotein complex consisting of WAVE, PIR121/Sra-1, Nap1, Abi-2 and HSPC300 mediates responsiveness of WAVE to upstream regulators such as Rac. Essential roles in WAVE complex assembly or function have been demonstrated for PIR121/Sra-1, Nap1 and Abi-2, but the significance of HSPC300 in this complex is unclear. Plant homologs of all mammalian WAVE complex components have been identified, including HSPC300, the mammalian homolog of maize BRICK1 (BRK1). We show that, like mutations disrupting the Arabidopsis homologs of PIR121/Sra-1, Nap1 and Scar/WAVE, mutations in the Arabidopsis BRK1gene result in trichome and pavement cell morphology defects (and associated alterations in the F-actin cytoskeleton of expanding cells) similar to those caused by mutations disrupting the ARP2/3 complex itself. Analysis of double mutants provides genetic evidence that BRK1 functions in a pathway with the ARP2/3 complex. BRK1 is required for accumulation of SCAR1 protein in vivo,potentially explaining the apparently essential role of BRK1 in ARP2/3 complex function. |
Databáze: | OpenAIRE |
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