“Defining the molecular nature of the mitochondrial permeability transition pore(s)"​

Dear All,

Hope this email finds you well.

On behalf of the program in Mitochondria Biology & Intermediary Metabolism we would like to invite you to the Special Seminar:

“Defining the molecular nature of the mitochondrial permeability transition pore(s)"​

by Prof. Paolo Bernardi, MD

hosted by Dr. Elizabeth Jonas

on 12^th Nov. from 2:00- 3:00 pm in BOYER 206/208

Prof. Bernardi did the majority of the discovery in the field to characterize the mitochondrial permeability transition pore (mPTP) including finding the divalent sensitivity of permeability transition, the ROS sensitivity, and describing the cypD binding site on the ATP synthase. With over 300 publications, he is a champion of and leader in mitochondrial biology and has raised the fascination with mPTP to a fever pitch.

Background: The mitochondrial permeability transition is a Ca²⁺- and cyclophilin D (CypD)-facilitated increase of inner mitochondrial membrane permeability that allows diffusion of large molecules into mitochondria. Opening the mPTP causes mitochondrial swelling and eventually rupturing the outer membrane that can lead to apoptotic and necrotic cell death, particularly relevant in ischemic and degenerative disease. However, transient mPTP opening contributes physiological roles such as alterations in mitochondrial bioenergetics and rapid Ca2+ efflux. Both the adenine nucleotide translocase (ANT) and, more recently, the mitochondrial F₁F₀ (F)-ATP synthase dimers, monomers or c-subunit ring alone have been implicated in formation of the mPTP. Models for the molecular identity of the mPTP and the mechanisms underlying its opposing roles in the life and death of cells with in-depth insights into current controversies will be discussed.