The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission

By Ruchika Anand, T. Wai, M. Baker, Nikolay Kladt, A. Schauss, E. Rugarli, T. Langer. Journal of Cell Biology, 2014

762 citations recorded by the source corpus.

OPA1 processing by YEM1L and OMA1 is dispensable for mitochondrial fusion and instead drives mitochondrial fragmentation, which is crucial for mitochondrial integrity and quality control.

Subfields: Clinical Biochemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1fb348f50feb43b51fba531ef1b8a478e1a27892

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In Clinical Biochemistry

1. Prashant Mishra
2. Wen Chen
3. Yongsheng Li
4. Huakan Zhao
5. D. C. Chan
6. Hsiuchen Chen
7. B. Westermann

In Molecular Biology

1. Prashant Mishra
2. Huakan Zhao
3. Wen Chen
4. Yongsheng Li
5. D. C. Chan
6. Hsiuchen Chen
7. B. Westermann
8. J. Nunnari

Citations in the corpus

• Metabolic regulation of mitochondrial dynamics (2016, background): “It should be noted that cells lacking Yme1L and Oma1 do retain residual mitochondrial fusion activity (Anand et al., 2014) and more work will be needed to dissect how inner-membrane fusion is regulated in this situation.”
• Mitochondrial dynamics in health and disease: mechanisms and potential targets (2023, background): “L-Opa1 is proteolytically hydrolyzed to S-Opa1 by OMA1 and YME1 Like 1 ATPase (YME1Ll), and the relative levels of L-Opa1 and S-Opa1 are a key factor in determining the viability of mitochondrial fusion.(65) In addition to controlling the IMM fusion, Opa1 also orchestrates cristae integrity, mtDNA m”