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Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress

Open access
Rainbolt, T. Kelly, Lebeau, Justine, Puchades, Cristina, Wiseman, R. Luke·2016·Cell Reports

Abstract

The mitochondrial inner membrane proteases YME1L and OMA1 are critical regulators of essential mitochondrial functions, including inner membrane proteostasis maintenance and mitochondrial dynamics. Here, we show that YME1L and OMA1 are reciprocally degraded in response to distinct types of cellular stress. OMA1 is degraded through a YME1L-dependent mechanism in response to toxic insults that depolarize the mitochondrial membrane. Alternatively, insults that depolarize mitochondria and deplete cellular ATP stabilize active OMA1 and promote YME1L degradation. We show that the differential degradation of YME1L and OMA1 alters their proteolytic processing of the dynamin-like GTPase OPA1, a critical regulator of mitochondrial inner membrane morphology, which influences the recovery of tubular mitochondria following membrane-depolarization-induced fragmentation. Our results reveal the differential stress-induced degradation of YME1L and OMA1 as a mechanism for sensitively adapting mitochondrial inner membrane protease activity and function in response to distinct types of cellular insults.

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Metadata

Authors
Rainbolt, T. K., Lebeau, J., Puchades, C., & Wiseman, R. L.
Venue
Cell Reports
Publisher
Elsevier BV
Published
2016-03
Volume
14
Issue
9
Pages
2041-2049
ISSN
2211-1247 (ISSN-L)
OpenAlex
W2287576325
Cited by
167
References
9
FWCI
7.37
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress. https://app.cochat.ai/papers/10.1016/j.celrep.2016.02.011
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Rainbolt, T. K., Lebeau, J., Puchades, C., & Wiseman, R. L. (2016). Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress. Cell Reports. https://doi.org/10.1016/j.celrep.2016.02.011

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