Join us at the annual AIM Center Symposium on Friday, February 22, 2019 for a day of plenary talks and workshops by leading autophagy scientists from around the world.
The symposia, hosted by Drs. Vojo Deretic (AIM Center Director), Leon Murphy (Casma Therapeutics, USA), and Li Yu (Tsinghua University, China), will take place in the Domenici Center Auditorium at the Health Sciences Center, University of New Mexico. This event will follow the 2019 Keystone autophagy meeting in Santa Fe. To register (free) for the AIM satellite symposium, click here, otherwise, click below for the full list of speakers and additional information!
The AIM Center held it's first official annual meeting on May 21st, 2018, where the focus was on inflammation and metabolism research.
We had the pleasure of having guest speakers Philipp Scherer, PhD, Vishva Dixit, MD, Beth Levine's postdoctoral student - Salwa Sebti, PhD, and Danielle Sliter, PhD.
"Recently, NIH has funded a center for autophagy research named the Autophagy, Inflammation, and Metabolism (AIM) Center of Biomedical Research Excellence, located at the University of New Mexico Health Science Center (UNM HSC), with aspirations to promote autophagy research locally, nationally, and internationally."
Check out the editorial article in the journal of Autophagy.
RAC3 is a member of the p160 family of steroid receptor coactivators and it is highly expressed in several human cancers, contributing to enhanced cell proliferation and cellular transformation...
At high cell density or when plated on soft matrix, YAP/TAZ are redistributed from the nucleus to the cytosol, becoming transcriptionally inactive. Here the authors show that at high cell density, autophagosome formation is impaired due to reduced YAP/TAZ-dependent transcription of actomyosin gene
During autophagy, phagophores elongate to form double-membrane vesicles but the mechanism behind their closure is unknown. Here, the authors develop an autophagy assay and find a role for the endosomal sorting complexes required for transport component CHMP2A as a phagophore closure regulator.
Many Amyotrophic Lateral Sclerosis (ALS)-linked mutations cause accumulation of stress granules, and most ALS cases are caused by repeat expansions in C9ORF72. Here the authors show that C9ORF72 and the autophagy receptor p62 interact to associate with proteins symmetrically dimethylated on arginines such as FUS, to eliminate stress granules by autophagy.