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TurboID-based proximity labeling to identify LONP1-targeting proteins

ABSTRACT: It is documented that intracellular succinate levels are maintained and regulated by mitochondrial complexes II. In order to define the LONP1-dependent regulators of succinate content, unbiased TurboID-based proximity labeling was employed to exploit LONP1-targeting proteins. Our results showed that 63.5% of the proteins identified by LONP1-N-TurboID-based proximity labeling are mitochondrial proteins. Functional protein association networks analysis of the identified proteins indicated that these biotinylated proteins are related to carboxylic acid metabolic process, mitochondrial organization and mitochondrial gene expression.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Lei Fang

LAB HEAD: Lei Fang

PROVIDER: PXD031197 | Pride | 2023-04-08

REPOSITORIES: Pride

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Project description:This experiment was conducted to identify the mitochondrial protein changes in the presence and absence of LONP1 in skeletal muscle. The following abstract from the submitted manuscript describes the major findings of this work.Disuse-associated loss of muscle LONP1 impairs mitochondrial quality and causes reduced skeletal muscle mass and strength. Zhisheng Xu, Tingting Fu, Qiqi Guo, Danxia Zhou, Wanping Sun, Zheng Zhou, Lin Liu, Liwei Xiao, Yujing Yin, Yuhuan Jia, Xin Pan, Lei Fang, Min-sheng Zhu, Wenyong Fei, Bin Lu and Zhenji Gan. Mitochondrial proteolysis is an evolutionarily conserved quality control mechanism to maintain proper mitochondrial integrity and function. However, the physiological relevance of stress-induced impaired mitochondrial protein quality remains unclear. Here, we demonstrate that LONP1, a major mitochondrial protease resides in the matrix, plays a critical role in controlling mitochondrial quality as well as skeletal muscle mass and strength in response to muscle disuse. In humans and mice, disuse-related muscle loss is associated with decreased mitochondrial LONP1 protein. Skeletal muscle-specific ablation of LONP1 in mice resulted in impaired mitochondrial protein turnover, leading to mitochondrial dysfunction. This caused reduced muscle fiber size and strength. Mechanistically, aberrant accumulation of mitochondrial-retained protein in muscle upon loss of LONP1 induces the activation of autophagy-lysosome degradation program of muscle loss. Overexpressing a mitochondrial-retained mutant ornithine transcarbamylase (ΔOTC), a known protein degraded by LONP1, in skeletal muscle induces mitochondrial dysfunction, autophagy activation, and cause muscle loss and weakness. Thus, these findings reveal a pivotal role of LONP1-dependent mitochondrial protein quality-control in safeguarding mitochondrial function and preserving skeletal muscle mass and strength, and unravel an intriguing link between mitochondrial protein quality and muscle mass maintenance during muscle disuse.

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	20191030_01.wiff	Wiff
	20191030_01.wiff.scan	Wiff
	20191030_01_GZJ_N1.txt	Txt
	20191030_02.wiff	Wiff
	20191030_02.wiff.scan	Wiff

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TurboID-based proximity labeling to identify LONP1-targeting proteins

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