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

Research output: Contribution to journalArticleScientificpeer-review

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.
Original languageEnglish
JournalJournal of Cell Biology
Volume218
Issue number1
Pages (from-to)97-111
Number of pages15
ISSN0021-9525
DOIs
Publication statusPublished - 7 Jan 2019
MoE publication typeA1 Journal article-refereed

Fields of Science

  • MEMBRANE CURVATURE
  • CONTACT SITE
  • ATP SYNTHASE
  • CRISTAE
  • INSERTION
  • MIC10
  • GENERATION
  • MECHANISM
  • DYNAMICS
  • DIMER
  • 1182 Biochemistry, cell and molecular biology
  • 3111 Biomedicine

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