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Jan 11, 2023

RPG Seminar (2023-01-11)

Date: 11 January 2023 (Wednesday)

Time: 5:00 p.m. - 6:00 p.m.

Venue: Cheung Kung Hai Lecture Theatre 2, G/F, William M.W. Mong Block, 21 Sassoon Road


5:00 p.m.

Presenter: Mr. Wenjing LIU, PhD candidate
Primary Supervisor: Dr. You-qiang SONG
Presentation Title: Investigation of the effect of a nature compound in Alzheimer’s disease
Abstract: Alzheimer’s disease (AD) is the main cause of dementia and is quickly becoming one of the most expensive, lethal, and burdening disease in this century. Currently only a few drugs able to delay the progression of the disease and the treatments for AD primarily focus on controlling the symptoms and do not cure the disease because of its multiple forming mechanisms and the low bioavailability and low ability to cross the blood-brain barrier (BBB) of most potential drugs. Recently, we found a nature compound (YS6309) which can inhibit the phosphating of protein TAU by inhibiting E2F1-PAX6-GSK3beta pathway, we are now putting effort of the interplay of the compound and E2F1, and how exactly the binding of the compound regulates E2F1 expression and activity.


5:30 p.m.

Presenter: Ms. Jung Eun KIM, MPhil candidate
Primary Supervisor: Prof. Michael HUEN
Presentation Title: Role of H3K9me2 in transcriptional regulation on damaged chromatin
Abstract: DNA double-strand breaks (DSBs) trigger transient halting of nearby transcription during the repair process to protect genomic integrity. The timely suppression and restoration of local transcription is an integral DNA damage responses (DDR) process yet to be fully understood. Previously, the DYRK1B-EHMT2 pathway has been identified as a novel effector of DSB-induced transcription silencing. Briefly, DYRK1B kinase phosphorylates histone methyltransferase EHMT2 to promote its recruitment to the damaged chromatin, which in turn suppresses the local gene transcription. Here, we reveal that EHMT2 catalyzes di-methylation on Histone H3 lysine residue 9 (H3K9me2), a repressive epigenetic modification, to suppress transcription on DSB-bearing chromatin. Furthermore, we show that PHF8, an H3K9me2 demethylase, facilitates the resumption of transcription following repair. Together, we propose that the interplay between EHMT2 and PHF8 regulates the DSB-associated H3K9me2 dynamics that control transcription activity during the repair.


Should you have any enquiries, please feel free to contact Miss Cynthia Cheung at 3917 9748.