Michael Hothorn

This study identifies a minimal C-terminal targeting motif for plant catalases that enables their peroxisomal import in Arabidopsis.

The paper quantifies BR receptor binding kinetics and identifies key chemical features for receptor recognition, revealing structural plasticity and functional diversity in BR signaling.

This study reclassifies plant Kelch phosphatases as PP1-like serine/threonine phosphatases involved in cell cycle regulation rather than tyrosine phosphatases in brassinosteroid signaling.

The paper reports the crystal structure of the SRF6 ectodomain from Arabidopsis, obtained using a novel LRR crystallization screen, revealing structural features and potential signaling roles outside the brassinosteroid pathway.

The paper identifies PP-InsP-interacting complexes in Arabidopsis, including CK2 subunits, and shows InsP6 modulates CK2 activity by blocking substrate binding.

This study identifies a GAF signaling domain that regulates PPIP5K phosphatase activity in phosphate homeostasis through structural and functional analyses.

This study identifies three phosphatase families involved in inositol pyrophosphate catabolism in plants, showing their roles in growth, development, and nutrient signaling.