Postsynaptic densities (PSDs) are membrane semi-enclosed, submicron protein-enriched cellular compartments beneath postsynaptic membranes, which constantly exchange their components with bulk aqueous cytoplasm in synaptic spines. Formation and activity-dependent modulation of PSDs is considered as one of the most basic molecular events governing synaptic plasticity in the nervous system.
In this project, SynGAP, one of the most abundant PSD proteins and a Ras/Rap GTPase activator, has been discovered to form a homo-trimer and binds to multiple copies of PSD-95. Binding of SynGAP to PSD-95 induces phase separation of the complex, forming highly concentrated liquid-like droplets reminiscent of the PSD. The multivalent nature of the SynGAP/PSD-95 complex is critical for the phase separation to occur and for proper activity-dependent SynGAP dispersions from the PSD. In addition to revealing a dynamic anchoring mechanism of SynGAP at the PSD, the results also suggest a model for phase-transition-mediated formation of PSD.
- Kerry Holdings Professor of Science
- Chair Professor, Division of Life Science
- Senior Fellow, HKUST Jockey Club Institute for Advanced Study
- Director of Center of Systems Biology and Human Health
- Associate Director of State Key Laboratory of Molecular Neuroscience
An international research team co-led by HKUST, Beijing Neurosurgical Institute, and the Spanish National Cancer Research Center (CNIO) has discovered a mechanism that...
Researchers from HKUST discovered a novel molecular mechanism that controls the delivery of a key protein in planar cell polarity (PCP)...