Department of Chemistry Master Calendar

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This calendar includes all events from the following individual calendars: Department of Chemistry Alumni Events (events for an alumni audience), Department Events (events of general interest and/or relevant to all Chemistry research areas), Diversity, Equity, and Inclusion Events, Public Events, and events related to Chemistry research areas and programs (Analytical Chemistry, Chemical Biology, Chemistry-Biology Interface Training Program, Inorganic Chemistry & Materials Chemistry, Organic Chemistry, Physical Chemistry), as well as Department of Chemical and Biomolecular Engineering Seminars & Events.


Professor Luke Chao, Harvard University, "Ultrastructural regulation of the mitochondrial inner-membrane"

Event Type
Beckman 3269
Apr 29, 2024   3:00 pm  
Lisa Johnson
Originating Calendar
Chemistry - Physical Chemistry Seminars

Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms: a membrane-anchored long form (l-Opa1) and a processed short form (s-Opa1). We previously used an in vitro supported-lipid bilayer reconstitution system to show that stoichiometric levels of the processed, short form of Opa1 (s-Opa1) work together with l-Opa1 to mediate efficient and fast membrane pore opening (Ge et al., eLife 2020). Our understanding of the mechanisms for how Opa1 form influences cristae shape has remained less well defined. We performed in situ cryo-electron tomography of cryo-focused ion beam milled mammalian cells with well-defined Opa1 states to understand how each form of Opa1 influences cristae architecture. We describe differences in cristae geometry, membrane spacings, and subcompartment volumes. We find the absence of l-Opa1 results in mitochondria with wider cristae junctions and cells less sensitive to apoptotic stimuli, implicating l-Opa1 mediating the cytochrome c release process via the cristae junction. We discuss the implications Opa1-dependent ultrastructure in organelle function.


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