Plasma membrane-associated SCAR complex subunits promote cortical F-actin accumulation and normal growth characteristics in Arabidopsis roots
| Autor: | Julia Dyachok, Stevan Djakovic, Michelle R Facette, Kevin C. Vaughn, Laurie G. Smith, Mon-Ray Shao, Andrew J. Bowling, Lauren G. Clark |
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| Rok vydání: | 2009 |
| Předmět: |
0106 biological sciences
Recombinant Fusion Proteins Arabidopsis macromolecular substances Plant Science Biology 01 natural sciences Cell junction Plant Roots Actin-Related Protein 2-3 Complex Cell membrane 03 medical and health sciences Cell Wall Microsomes Botany medicine Cytoskeleton Molecular Biology Actin 030304 developmental biology 0303 health sciences Cell morphogenesis Arabidopsis Proteins Plant Extracts Cell Membrane Membrane Proteins Actins Cell biology Protein Subunits medicine.anatomical_structure Membrane protein SCAR complex Multiprotein Complexes Mutation 010606 plant biology & botany Protein Binding |
| Zdroj: | Molecular plant. 1(6) |
| ISSN: | 1674-2052 |
| Popis: | The ARP2/3 complex, a highly conserved nucleator of F-actin polymerization, and its activator, the SCAR complex, have been shown to play important roles in leaf epidermal cell morphogenesis in Arabidopsis. However, the intracellular site(s) and function(s) of SCAR and ARP2/3 complex-dependent actin polymerization in plant cells remain unclear. We demonstrate that putative SCAR complex subunits BRK1 and SCAR1 are localized to the plasma membrane at sites of cell growth and wall deposition in expanding cells of leaves and roots. BRK1 localization is SCAR-dependent, providing further evidence of an association between these proteins in vivo. Consistent with plasma membrane localization of SCAR complex subunits, cortical F-actin accumulation in root tip cells is reduced in brk1 mutants. Moreover, mutations disrupting the SCAR or ARP2/3 complex reduce the growth rate of roots and their ability to penetrate semi-solid medium, suggesting reduced rigidity. Cell walls of mutant roots exhibit abnormal structure and composition at intercellular junctions where BRK1 and SCAR1 are enriched in the adjacent plasma membrane. Taken together, our results suggest that SCAR and ARP2/3 complex-dependent actin polymerization promotes processes at the plasma membrane that are important for normal growth and wall assembly. |
| Databáze: | OpenAIRE |
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