Search bioRxiv⌕ Search

Biology subjects

Baquero Forero, A.

Publications and source records attributed to Baquero Forero, A..

2 recordsLinked to original sources

In vivo imaging uncovers an abundant but rarely active pool of plant ARP2/3 complexes associated with exocyst complex subunit

The ARP2/3 complex generates branched actin networks that regulate membrane dynamics across eukaryotes. In plants, ARP2/3 is activated primarily by the WAVE/SCAR complex and is essential for cell morphogenesis, yet its spatiotemporal behavior in living cells remains poorly understood. Using high-resolution live-cell microscopy, we found that, in addition to their previously reported stable accumulation at three-way cell junctions and peroxisomes, WAVE/SCAR and ARP2/3 subunits also form abundant, highly dynamic, short-lived assemblies in the cortical cytoplasm, with lifetimes of only a few seconds. Genetic and colocalization analyses further revealed that only a minority of observed complexes are fully assembled and active, indicating that plant cells maintain a large pool of partially assembled or inactive ARP2/3 structures. Our data indicate that microtubules influence the abundance of cortical assemblies, whereas actin primarily affects their dynamics. Importantly, our analysis demonstrated a spatial and functional association between dynamic ARP2/3 foci and exocytotic events at the plasma membrane. Together, our findings suggest that the cytoplasm of plant epidermal cells contains a large reservoir of ARP2/3 complexes whose localized activation is tightly regulated and associated with membrane trafficking.

plant biology↗

Comprehensive comparative assessment of the Arabidopsis thaliana MLO2-calmodulin interaction by various in vitro and in vivo protein-protein interaction assays

Mildew resistance locus o (MLO) proteins are heptahelical integral membrane proteins of which some isoforms act as susceptibility factors for the fungal powdery mildew pathogen. In many angiosperm plant species, loss-of-function mlo mutants confer durable broad-spectrum resistance against the powdery mildew disease. Barley Mlo is known to interact via a cytosolic carboxyl-terminal domain with the intracellular calcium sensor calmodulin (CAM) in a calcium-dependent manner. Site-directed mutagenesis has revealed key amino acid residues in the barley Mlo calcium-binding domain (CAMBD) that, when mutated, affect the MLO-CAM association. We here tested the respective interaction between Arabidopsis thaliana MLO2 and CAM2 using seven different types of in vitro and in vivo protein-protein interaction assays. In each assay, we deployed a wild-type version of either the MLO2 carboxyl terminus (MLO2CT), harboring the CAMBD, or the MLO2 full-length protein and corresponding mutant variants in which two key residues within the CAMBD were substituted by non-functional amino acids. We focused in particular on the substitution of two hydrophobic amino acids (LW/RR mutant) and found in most protein-protein interaction experiments reduced binding of CAM2 to the corresponding MLO2/MLO2CT LW/RR mutant variants in comparison to the respective wild-type versions. However, the Ura3-based yeast split-ubiquitin system and in planta bimolecular fluorescence complementation (BiFC) assays failed to indicate reduced CAM2 binding to the mutated CAMBD. Our data shed further light on the interaction of MLO and CAM proteins and provide a comprehensive comparative assessment of different types of protein-protein interaction assays with wild-type and mutant versions of an integral membrane protein.

plant biology↗