FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function

Liang Wang, Ziyi Yan, Helena Vihinen, Ove Eriksson, Weihuan Wang, Rabah Soliymani, Yao Lu, Yaxin Xue, Eija Jokitalo, Hongxia Zhao

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

Kuvaus

Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.
Alkuperäiskielienglanti
LehtiJournal of Cell Biology
Vuosikerta218
Numero1
Sivut97-111
Sivumäärä15
ISSN0021-9525
DOI - pysyväislinkit
TilaJulkaistu - 7 tammikuuta 2019
OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

Tieteenalat

  • 1182 Biokemia, solu- ja molekyylibiologia
  • 3111 Biolääketieteet

Lainaa tätä

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title = "FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function",
abstract = "Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.",
keywords = "MEMBRANE CURVATURE, CONTACT SITE, ATP SYNTHASE, CRISTAE, INSERTION, MIC10, GENERATION, MECHANISM, DYNAMICS, DIMER, 1182 Biochemistry, cell and molecular biology, 3111 Biomedicine",
author = "Liang Wang and Ziyi Yan and Helena Vihinen and Ove Eriksson and Weihuan Wang and Rabah Soliymani and Yao Lu and Yaxin Xue and Eija Jokitalo and Hongxia Zhao",
year = "2019",
month = "1",
day = "7",
doi = "10.1083/jcb.201806191",
language = "English",
volume = "218",
pages = "97--111",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "ROCKEFELLER UNIVERSITY PRESS",
number = "1",

}

FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function. / Wang, Liang; Yan, Ziyi; Vihinen, Helena; Eriksson, Ove; Wang, Weihuan; Soliymani, Rabah; Lu, Yao; Xue, Yaxin; Jokitalo, Eija; Zhao, Hongxia.

julkaisussa: Journal of Cell Biology, Vuosikerta 218, Nro 1, 07.01.2019, s. 97-111.

Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

TY - JOUR

T1 - FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function

AU - Wang, Liang

AU - Yan, Ziyi

AU - Vihinen, Helena

AU - Eriksson, Ove

AU - Wang, Weihuan

AU - Soliymani, Rabah

AU - Lu, Yao

AU - Xue, Yaxin

AU - Jokitalo, Eija

AU - Zhao, Hongxia

PY - 2019/1/7

Y1 - 2019/1/7

N2 - Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.

AB - Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.

KW - MEMBRANE CURVATURE

KW - CONTACT SITE

KW - ATP SYNTHASE

KW - CRISTAE

KW - INSERTION

KW - MIC10

KW - GENERATION

KW - MECHANISM

KW - DYNAMICS

KW - DIMER

KW - 1182 Biochemistry, cell and molecular biology

KW - 3111 Biomedicine

U2 - 10.1083/jcb.201806191

DO - 10.1083/jcb.201806191

M3 - Article

VL - 218

SP - 97

EP - 111

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 1

ER -