Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes - Laboratoire d'ingénierie des systèmes macromoléculaires Accéder directement au contenu
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2017

Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes

David Hoogerheide
  • Fonction : Auteur
Sergei Noskov
  • Fonction : Auteur
Daniel Jacobs
  • Fonction : Auteur
Vitalii Silin
  • Fonction : Auteur
David Worcester
  • Fonction : Auteur
Jeff Abramson
  • Fonction : Auteur
Hirsh Nanda
  • Fonction : Auteur
Tatiana Rostovtseva
  • Fonction : Auteur
Sergey Bezrukov
  • Fonction : Auteur

Résumé

Significance Tubulin has emerged as a highly unexpected component of mitochondrial membranes involved in regulation of membrane permeability. This discovery has reawakened interest in the nature of the tubulin–membrane interaction to answer a new question: How does tubulin, a cytosolic protein famous for its role in microtubule structure and dynamics, come to target mitochondrial membranes? Here, using a combination of five biophysical methods, we study peripheral binding of tubulin to biomimetic membranes of different lipid compositions. We conclude that tubulin distinguishes between lamellar and nonlamellar lipids through a highly conserved amphipathic binding motif. Specifically, α-tubulin targets cell and organelle membranes by sensing lipid-packing defects via an amphipathic α-helix, with broad consequences for both normal cellular function and disease.

Dates et versions

hal-03836318 , version 1 (02-11-2022)

Identifiants

Citer

David Hoogerheide, Sergei Noskov, Daniel Jacobs, Lucie Bergdoll, Vitalii Silin, et al.. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes. Proceedings of the National Academy of Sciences of the United States of America, 2017, 114 (18), ⟨10.1073/pnas.1619806114⟩. ⟨hal-03836318⟩
12 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More