The identities of enzymes: study further defines the function of a potential target for Alzheimer’s therapy

A new study from the lab of UW-Madison professor of medicine Luigi Puglielli, MD, PhD, opens a door to potential treatments for diseases of age, such as Alzheimer’s disease, by defining the roles of two enzymes that are imperative to protein production. “Endoplasmic reticulum acetyltransferases Atase1 and Atase2 differentially regulate reticulophagy, macroautophagy and cellular acetyl-CoA metabolism” was published in April in the journal Communications Biology.

Luigi Puglielli, MD, PhD – Slide of the Week

Nε-lysine acetylation in the ER is an essential component of the quality control machinery. ER acetylation is ensured by a membrane transporter, AT-1/SLC33A1, which translocates cytosolic acetyl-CoA into the ER lumen, and two acetyltransferases, ATase1 and ATase2, which acetylate nascent polypeptides within the ER lumen. Dysfunctional AT-1, as caused by gene mutation or duplication events, results in severe disease phenotypes. 

Luigi Puglielli, MD, PhD – Slide of the Week

Nε-lysine acetylation of nascent glycoproteins within the endoplasmic reticulum (ER) lumen regulates the efficiency of the secretory pathway. The ER acetylation machinery consists of the membrane transporter, acetyl-CoA transporter 1 (AT-1/SLC33A1), and two acetyltransferases, ATase1/NAT8B and ATase2/NAT8. Dysfunctional ER acetylation is associated with severe neurological diseases with duplication of AT-1/SLC33A1 being associated with autism spectrum disorder, intellectual disability, and dysmorphism.

Proposals by Waisman investigators selected for UW-Madison Cluster Hire Initiative

Several Waisman Center investigators played key roles in crafting research proposals that were recently selected as ‘cluster hires’ by the University of Wisconsin-Madison. UW–Madison’s Cluster Hiring Initiative was launched in 1998 as an innovative partnership …