U. Hohmann

Mechanistic insights into the function of 14-3-3 proteins as negative regulators of brassinosteroid signaling in Arabidopsis.

This study identifies 14-3-3 binding sites in BR signaling components and shows their role as negative regulators in Arabidopsis.

Phosphorylation and ubiquitination independent endocytosis of BRI1

This study shows that a BR-binding-deficient BRI1 mutant is internalized similarly to wild-type BRI1, suggesting parallel endocytic routes and non-canonical functions.

Constitutive activation of leucine-rich repeat receptor kinase signaling pathways by BAK1-interacting receptor-like kinase 3 chimera

The paper reports that chimeric receptor proteins formed by fusing BIR3 LRR domains with SERK-dependent LRR-RK kinase domains activate signaling pathways constitutively, leading to gain-of-function phenotypes.

Molecular mechanism for the recognition of sequence-divergent CIF peptides by the plant receptor kinases GSO1/SGN3 and GSO2.

This paper identifies the molecular mechanism by which plant receptor kinases GSO1/SGN3 and GSO2 recognize sequence-divergent CIF peptides through structural and biochemical analyses.

Crystal structure of the LRR ectodomain of the plant immune receptor kinase SOBIR1.

The paper reports the crystal structure of the LRR ectodomain of the plant immune receptor kinase SOBIR1, revealing unique capping domains and potential protein-protein interaction sites.

Molecular characterization of CHAD domains as inorganic polyphosphate binding modules

This study identifies CHAD domains as specific inorganic polyphosphate binding modules across bacteria, archaea, and eukaryotes, revealing their structural and functional roles in polyP metabolism and localization.

Mechanistic analysis of the SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signaling

The paper investigates the role of the SERK3 elongated allele in brassinosteroid signaling, finding that it disrupts BIR ectodomain interactions with co-receptors rather than enhancing BRI1 binding.