This study identified paxillin as an activity-dependent nuclear regulator of alternative splicing during the postnatal critical period. It established a mechanistic link between synaptic activity, paxillin S119 phosphorylation, and critical-period splicing programs required for neural plasticity.

This work showed that ECM29/proteasome-dependent antigen generation in CNS-resident neuroglia helps shape the self-antigen landscape and promotes regulatory T cell activation. It extended my proteostasis research into CNS immune tolerance and neuroimmune regulation.

This study demonstrated that paxillin and drebrin form a softness-dependent module that mediates BDNF-induced force transduction and growth cone turning in soft brain-like environments. I led the project concept and integrated the mechanobiology, imaging, and developmental analyses.

This work showed that ECM29-dependent proteasome localization regulates local NKCC1 abundance, the timing of the excitatory-to-inhibitory GABA switch, and neuronal excitability during development. It extended my proteasome program from axon biology to functional circuit maturation.

This study identified a neuronal paxillin mechanism adapted to soft, brain-like mechanical environments and showed that paxillin promotes neurite initiation through interaction with the endocytic machinery. It established neuronal mechanobiology as a major direction of my independent research program.

This study identified ECM29 as a key adaptor linking proteasomes to long-range transport in developing neurons and showed that stage-dependent proteasome positioning contributes directly to axon development. It established the proteasome-distribution program as a major axis of my laboratory.