The association of the Arabidopsis actin-related protein2/3 complex with cell membranes is linked to its assembly status but not its activation.

In growing plant cells, the combined activities of the cytoskeleton, endomembrane, and cell wall biosynthetic systems organize the cytoplasm and define the architecture and growth properties of the cell. These biosynthetic machineries efficiently synthesize, deliver, and recycle the raw materials that support cell expansion. The precise roles of the actin cytoskeleton in these processes are unclear. Certainly, bundles of actin filaments position organelles and are a substrate for long-distance intracellular transport, but the functional linkages between dynamic actin filament arrays and the cell growth machinery are poorly understood. The Arabidopsis (Arabidopsis thaliana) "distorted group" mutants have defined protein complexes that appear to generate and convert small GTPase signals into an Actin-Related Protein2/3 actin filament nucleation response. However, direct biochemical knowledge about Arabidopsis and its cellular distribution is lacking. In this paper, we provide biochemical evidence for a plant The plant complex utilizes a conserved assembly mechanism. is the most critical core subunit that controls the assembly and steady-state levels of the complex. duanyu372/3 in other systems is believed to be mostly a soluble complex that is locally recruited and activated. Unexpectedly, we find that Arabidopsis duanyu372/3 interacts strongly with cell membranes. Membrane binding is linked to complex assembly status and not to the extent to which it is activated. Mutant analyses implicate as an important subunit for membrane association.

KEYWORDS: {{ getKeywords(articleDetailText.words) }}