Alberto P. Macho

This study identifies a phosphorylation-dependent mechanism by which BIK1 regulates TTL3 to control cellulose biosynthesis under salt stress.

This study determines the structure of the plant receptor IGP1 bound to a cellulose-derived DAMP, revealing its mechanism for recognizing glycan patterns and initiating immune responses.

This study identifies RipAV, an effector from Ralstonia solanacearum, as a protein that targets plant PUB proteins and CPK28 to suppress immunity by promoting BIK1 degradation.

This study identifies how the bacterial effector RipE1 stabilizes by hijacking plant ubiquitin proteases and phosphorylation, avoiding degradation and promoting bacterial survival.

This study identifies distinct biological roles of plant synaptotagmins, showing SYT1 and SYT3 are involved in abiotic stress resistance while SYT5 is linked to pathogen resistance.

The paper shows that synaptotagmins maintain diacylglycerol homeostasis at ER-PM contact sites during abiotic stress by preventing its detrimental accumulation at the plasma membrane.

This study identifies TTL proteins as scaffolds for BR signaling components in Arabidopsis, enhancing signal transduction by localizing these components at the plasma membrane upon BR treatment.