תאריך:
ד', 25/11/202016:00-17:00
מיקום:
Zoom
Dr. Raul Zavaliev
Department of Biology
Duke University
Protein Condensation as Cell Survival Strategy in Plant Immunity
Zoom meeting
Meeting ID: 899 9888 8303
Passcode: 966627
Abstract:
In plants, pathogen effector-triggered immunity (ETI) often leads to programmed cell death,
which is restricted by NPR1, an activator of systemic acquired resistance. However, the
biochemical activities of NPR1 enabling it to both promote defense and restrict cell death
remain unclear. In this work we show that NPR1 promotes cell survival by targeting
substrates for ubiquitination and degradation through formation of salicylic acid-induced
NPR1 condensates (SINCs). SINCs are enriched with stress response proteins, including
nucleotide-binding leucine-rich repeat immune receptors, oxidative and DNA damage
response proteins and protein quality control machineries. Transition of NPR1 into
condensates is required for the formation of the NPR1-Cullin 3 E3 ligase complex to
ubiquitinate SINC-localized substrates, such as EDS1 and other key immune regulators to
promote cell survival during ETI. Our analysis of SINCs suggests that NPR1 is centrally
integrated into the cell death/survival decisions in plant immunity by modulating multiple
stress-responsive processes in this quasi organelle.
Department of Biology
Duke University
Protein Condensation as Cell Survival Strategy in Plant Immunity
Zoom meeting
Meeting ID: 899 9888 8303
Passcode: 966627
Abstract:
In plants, pathogen effector-triggered immunity (ETI) often leads to programmed cell death,
which is restricted by NPR1, an activator of systemic acquired resistance. However, the
biochemical activities of NPR1 enabling it to both promote defense and restrict cell death
remain unclear. In this work we show that NPR1 promotes cell survival by targeting
substrates for ubiquitination and degradation through formation of salicylic acid-induced
NPR1 condensates (SINCs). SINCs are enriched with stress response proteins, including
nucleotide-binding leucine-rich repeat immune receptors, oxidative and DNA damage
response proteins and protein quality control machineries. Transition of NPR1 into
condensates is required for the formation of the NPR1-Cullin 3 E3 ligase complex to
ubiquitinate SINC-localized substrates, such as EDS1 and other key immune regulators to
promote cell survival during ETI. Our analysis of SINCs suggests that NPR1 is centrally
integrated into the cell death/survival decisions in plant immunity by modulating multiple
stress-responsive processes in this quasi organelle.