Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix

Yuichi Matsushima; Kazuya Takahashi; Song Yue; Yuki Fujiyoshi; Hideaki Yoshioka; Masamune Aihara; Daiki Setoyama; Takeshi Uchiumi; Satoshi Fukuchi; Dongchon Kang

doi:10.1038/s42003-021-02498-z

Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix

Yuichi Matsushima, Kazuya Takahashi, Song Yue, Yuki Fujiyoshi, Hideaki Yoshioka, Masamune Aihara, Daiki Setoyama, Takeshi Uchiumi, Satoshi Fukuchi, Dongchon Kang

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

Human ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes. Depletion of LONP1 causes aggregation of a broad range of proteins in the mitochondrial matrix and decreases the levels of their soluble forms. The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity. LONP1 forms a complex with the import machinery and an incoming protein, and protein aggregation is linked with matrix protein import. LONP1 also contributes to the degradation of imported, aberrant, unprocessed proteins using its protease activity. Taken together, our results show that LONP1 functions as a gatekeeper for specific proteins imported into the mitochondrial matrix.

Original language	English
Article number	974
Journal	Communications Biology
Volume	4
Issue number	1
DOIs	https://doi.org/10.1038/s42003-021-02498-z
Publication status	Published - Dec 2021

All Science Journal Classification (ASJC) codes

Medicine (miscellaneous)
General Biochemistry,Genetics and Molecular Biology
General Agricultural and Biological Sciences

Access to Document

10.1038/s42003-021-02498-z

Cite this

@article{484ffe31f65c42e8978a78905045f636,

title = "Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix",

abstract = "Human ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes. Depletion of LONP1 causes aggregation of a broad range of proteins in the mitochondrial matrix and decreases the levels of their soluble forms. The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity. LONP1 forms a complex with the import machinery and an incoming protein, and protein aggregation is linked with matrix protein import. LONP1 also contributes to the degradation of imported, aberrant, unprocessed proteins using its protease activity. Taken together, our results show that LONP1 functions as a gatekeeper for specific proteins imported into the mitochondrial matrix.",

author = "Yuichi Matsushima and Kazuya Takahashi and Song Yue and Yuki Fujiyoshi and Hideaki Yoshioka and Masamune Aihara and Daiki Setoyama and Takeshi Uchiumi and Satoshi Fukuchi and Dongchon Kang",

note = "Publisher Copyright: {\textcopyright} 2021, The Author(s).",

year = "2021",

month = dec,

doi = "10.1038/s42003-021-02498-z",

language = "English",

volume = "4",

journal = "Communications Biology",

issn = "2399-3642",

number = "1",

}

TY - JOUR

T1 - Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix

AU - Matsushima, Yuichi

AU - Takahashi, Kazuya

AU - Yue, Song

AU - Fujiyoshi, Yuki

AU - Yoshioka, Hideaki

AU - Aihara, Masamune

AU - Setoyama, Daiki

AU - Uchiumi, Takeshi

AU - Fukuchi, Satoshi

AU - Kang, Dongchon

PY - 2021/12

Y1 - 2021/12

N2 - Human ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes. Depletion of LONP1 causes aggregation of a broad range of proteins in the mitochondrial matrix and decreases the levels of their soluble forms. The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity. LONP1 forms a complex with the import machinery and an incoming protein, and protein aggregation is linked with matrix protein import. LONP1 also contributes to the degradation of imported, aberrant, unprocessed proteins using its protease activity. Taken together, our results show that LONP1 functions as a gatekeeper for specific proteins imported into the mitochondrial matrix.

AB - Human ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes. Depletion of LONP1 causes aggregation of a broad range of proteins in the mitochondrial matrix and decreases the levels of their soluble forms. The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity. LONP1 forms a complex with the import machinery and an incoming protein, and protein aggregation is linked with matrix protein import. LONP1 also contributes to the degradation of imported, aberrant, unprocessed proteins using its protease activity. Taken together, our results show that LONP1 functions as a gatekeeper for specific proteins imported into the mitochondrial matrix.

UR - http://www.scopus.com/inward/record.url?scp=85112695776&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85112695776&partnerID=8YFLogxK

U2 - 10.1038/s42003-021-02498-z

DO - 10.1038/s42003-021-02498-z

M3 - Article

C2 - 34400774

AN - SCOPUS:85112695776

SN - 2399-3642

VL - 4

JO - Communications Biology

JF - Communications Biology

IS - 1

M1 - 974

ER -

Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this