EMD-43051

Tomography
EMD-43051 Deposition: 07/12/2023
Map released: 31/01/2024
Last modified: 14/02/2024
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EMD-43051

cryo-electron tomogram of mitochondria in cryo-FIB milled l-Opa1* mouse embryonic fibroblasts

EMD-43051

Tomography
EMD-43051 Deposition: 07/12/2023
Map released: 31/01/2024
Last modified: 14/02/2024
Overview Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Mus musculus
Sample: mitochondria in mouse embryonic fibroblasts with OMA1 deletion and OPA1-exon5b deletion
Raw data: EMPIAR-11819

Deposition Authors: Fry MY , Navarro PP , Ananda VY , Ge Y , McDonald JL , Hakim P , Luce BE , Lugo CM , Chao LH
In situ architecture of Opa1-dependent mitochondrial cristae remodeling.
PUBMED: 38225406
DOI: doi:10.1038/s44318-024-00027-2
ISSN: 1460-2075
ASTM: EMJODG
Abstract:
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 in the mitochondrion, a membrane-anchored long form (l-Opa1) and a processed short form (s-Opa1). The mechanisms for how Opa1 influences cristae shape have remained unclear due to lack of native three-dimensional views of cristae. We perform in situ cryo-electron tomography of cryo-focused ion beam milled mouse embryonic fibroblasts with defined Opa1 states to understand how each form of Opa1 influences cristae architecture. In our tomograms, we observe a variety of cristae shapes with distinct trends dependent on s-Opa1:l-Opa1 balance. Increased l-Opa1 levels promote cristae stacking and elongated mitochondria, while increased s-Opa1 levels correlated with irregular cristae packing and round mitochondria shape. Functional assays indicate a role for l-Opa1 in wild-type apoptotic and calcium handling responses, and show a compromised respiratory function under Opa1 imbalance. In summary, we provide three-dimensional visualization of cristae architecture to reveal relationships between mitochondrial ultrastructure and cellular function dependent on Opa1-mediated membrane remodeling.