Protein acylation-deacylation cycles in cancer and inflammation

Title:

Protein acylation-deacylation cycles in cancer and inflammation

Schedule:

Date: 9^th October, 2023 (Mon)

Time: 5:30 - 6:30 pm (HKT)

Venue: Lecture Theatre P1, Chong Yuet Ming Chemistry Building

Speaker:

Prof. Hening LIN

Department of Chemistry and Chemical Biology

Cornell University

Abstract:

Protein post-translational modifications play important roles in cell signaling and stress response. My lab has been studying the regulatory roles of protein acylation, which was led by the sirtuins family of enzymes that are NAD+-dependent protein lysine deacylases. They were initially considered to be deacetylases, but we and others later found that many of them can remove other acyl groups, such as succinyl and long chain fatty acyl groups. Interestingly, SIRT2, a mammalian sirtuin that is mainly localized in the cytosol, is able to remove both acetyl and myristoyl/palmitoyl groups very efficiently. We discovered that the deacylation activity regulates several Ras super family of small GTPases. Through these studies, we found interesting examples that an acylation-deacylation cycle promotes cell signaling. Thus, inhibiting acylation and inhibiting deacylation produce the same biological effect. This cycling effect is different from the commonly known on-off switch effect of protein modifications and offers new opportunities to understand cell signaling and treat human diseases, including cancer and inflammation.

- ALL ARE WELCOME -