Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components

Yakubu Princely Abudu; Birendra Kumar Shrestha; Wenxin Zhang; Anthimi Palara; Hanne Britt Brenne; Kenneth Bowitz Larsen; Deanna Lynn Wolfson; Gianina Dumitriu; Cristina Ionica Øie; Balpreet Singh Ahluwalia; Gahl Levy; Christian Behrends; Sharon A. Tooze; Stephane Mouilleron; Trond Lamark; Terje Johansen

doi:10.1083/jcb.202009092

Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components

Yakubu Princely Abudu, Birendra Kumar Shrestha, Wenxin Zhang, Anthimi Palara, Hanne Britt Brenne, Kenneth Bowitz Larsen, Deanna Lynn Wolfson, Gianina Dumitriu, Cristina Ionica Øie, Balpreet Singh Ahluwalia, Gahl Levy, Christian Behrends, Sharon A. Tooze, Stephane Mouilleron, Trond Lamark, Terje Johansen

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

Abstract

Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stressinduced mitophagy, basal mitophagy processes exert organelle quality control. Here, we show that the sorting and assembly machinery (SAM) complex protein SAMM50 interacts directly with ATG8 family proteins and p62/SQSTM1 to act as a receptor for a basal mitophagy of components of the SAM and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 regulates mitochondrial architecture by controlling formation and assembly of the MICOS complex decisive for normal cristae morphology and exerts quality control of MICOS components. To this end, SAMM50 recruits ATG8 family proteins through a canonical LIR motif and interacts with p62/SQSTM1 to mediate basal mitophagy of SAM and MICOS components. Upon metabolic switch to oxidative phosphorylation, SAMM50 and p62 cooperate to mediate efficient mitophagy.

Original language	English
Article number	e202009092
Journal	Journal of Cell Biology
Volume	220
Issue number	8
DOIs	https://doi.org/10.1083/jcb.202009092
State	Published - 22 Aug 2021
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2021 Abudu et al.

ASJC Scopus subject areas

Cell Biology

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10.1083/jcb.202009092

Cite this

Abudu, Y. P., Shrestha, B. K., Zhang, W., Palara, A., Brenne, H. B., Larsen, K. B., Wolfson, D. L., Dumitriu, G., Øie, C. I., Ahluwalia, B. S., Levy, G., Behrends, C., Tooze, S. A., Mouilleron, S., Lamark, T., & Johansen, T. (2021). Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components. Journal of Cell Biology, 220(8), Article e202009092. https://doi.org/10.1083/jcb.202009092

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title = "Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components",

abstract = "Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stressinduced mitophagy, basal mitophagy processes exert organelle quality control. Here, we show that the sorting and assembly machinery (SAM) complex protein SAMM50 interacts directly with ATG8 family proteins and p62/SQSTM1 to act as a receptor for a basal mitophagy of components of the SAM and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 regulates mitochondrial architecture by controlling formation and assembly of the MICOS complex decisive for normal cristae morphology and exerts quality control of MICOS components. To this end, SAMM50 recruits ATG8 family proteins through a canonical LIR motif and interacts with p62/SQSTM1 to mediate basal mitophagy of SAM and MICOS components. Upon metabolic switch to oxidative phosphorylation, SAMM50 and p62 cooperate to mediate efficient mitophagy.",

author = "Abudu, {Yakubu Princely} and Shrestha, {Birendra Kumar} and Wenxin Zhang and Anthimi Palara and Brenne, {Hanne Britt} and Larsen, {Kenneth Bowitz} and Wolfson, {Deanna Lynn} and Gianina Dumitriu and {\O}ie, {Cristina Ionica} and Ahluwalia, {Balpreet Singh} and Gahl Levy and Christian Behrends and Tooze, {Sharon A.} and Stephane Mouilleron and Trond Lamark and Terje Johansen",

note = "Publisher Copyright: {\textcopyright} 2021 Abudu et al.",

year = "2021",

month = aug,

day = "22",

doi = "10.1083/jcb.202009092",

language = "English",

volume = "220",

journal = "Journal of Cell Biology",

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Abudu, YP, Shrestha, BK, Zhang, W, Palara, A, Brenne, HB, Larsen, KB, Wolfson, DL, Dumitriu, G, Øie, CI, Ahluwalia, BS, Levy, G, Behrends, C, Tooze, SA, Mouilleron, S, Lamark, T & Johansen, T 2021, 'Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components', Journal of Cell Biology, vol. 220, no. 8, e202009092. https://doi.org/10.1083/jcb.202009092

TY - JOUR

T1 - Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components

AU - Abudu, Yakubu Princely

AU - Shrestha, Birendra Kumar

AU - Zhang, Wenxin

AU - Palara, Anthimi

AU - Brenne, Hanne Britt

AU - Larsen, Kenneth Bowitz

AU - Wolfson, Deanna Lynn

AU - Dumitriu, Gianina

AU - Øie, Cristina Ionica

AU - Ahluwalia, Balpreet Singh

AU - Levy, Gahl

AU - Behrends, Christian

AU - Tooze, Sharon A.

AU - Mouilleron, Stephane

AU - Lamark, Trond

AU - Johansen, Terje

PY - 2021/8/22

Y1 - 2021/8/22

N2 - Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stressinduced mitophagy, basal mitophagy processes exert organelle quality control. Here, we show that the sorting and assembly machinery (SAM) complex protein SAMM50 interacts directly with ATG8 family proteins and p62/SQSTM1 to act as a receptor for a basal mitophagy of components of the SAM and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 regulates mitochondrial architecture by controlling formation and assembly of the MICOS complex decisive for normal cristae morphology and exerts quality control of MICOS components. To this end, SAMM50 recruits ATG8 family proteins through a canonical LIR motif and interacts with p62/SQSTM1 to mediate basal mitophagy of SAM and MICOS components. Upon metabolic switch to oxidative phosphorylation, SAMM50 and p62 cooperate to mediate efficient mitophagy.

AB - Mitophagy is the degradation of surplus or damaged mitochondria by autophagy. In addition to programmed and stressinduced mitophagy, basal mitophagy processes exert organelle quality control. Here, we show that the sorting and assembly machinery (SAM) complex protein SAMM50 interacts directly with ATG8 family proteins and p62/SQSTM1 to act as a receptor for a basal mitophagy of components of the SAM and mitochondrial contact site and cristae organizing system (MICOS) complexes. SAMM50 regulates mitochondrial architecture by controlling formation and assembly of the MICOS complex decisive for normal cristae morphology and exerts quality control of MICOS components. To this end, SAMM50 recruits ATG8 family proteins through a canonical LIR motif and interacts with p62/SQSTM1 to mediate basal mitophagy of SAM and MICOS components. Upon metabolic switch to oxidative phosphorylation, SAMM50 and p62 cooperate to mediate efficient mitophagy.

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DO - 10.1083/jcb.202009092

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AN - SCOPUS:85107084680

SN - 0021-9525

VL - 220

JO - Journal of Cell Biology

JF - Journal of Cell Biology

IS - 8

M1 - e202009092

ER -

Samm50 acts with p62 in piecemeal basal- and oxphos-induced mitophagy of sam and micos components

Abstract

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