Two-Step Membrane Binding of NDPK-B Induces Membrane Fluidity Decrease and Changes in Lipid Lateral Organization and Protein Cluster Formation

Liberty Francois-Moutal, Myriam M. Ouberai, Ofelia Maniti, Mark E. Welland, Agnieszka Strzelecka-Kiliszek, Marcin Wos, Slawomir Pikula, Joanna Bandorowicz-Pikula, Olivier Marcillat, Thierry Granjon

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Nucleoside diphosphate kinases (NDPKs) are crucial elements in a wide array of cellular physiological or pathophysiological processes such as apoptosis, proliferation, or metastasis formation. Among the NDPK isoenzymes, NDPK-B, a cytoplasmic protein, was reported to be associated with several biological membranes such as plasma or endoplasmic reticulum membranes. Using several membrane models (liposomes, lipid monolayers, and supported lipid bilayers) associated with biophysical approaches, we show that lipid membrane binding occurs in a two-step process: first, initiation by a strong electrostatic adsorption process and followed by shallow penetration of the protein within the membrane. The NDPK-B binding leads to a decrease in membrane fluidity and formation of protein patches. The ability of NDPK-B to form microdomains at the membrane level may be related to protein-protein interactions triggered by its association with anionic phospholipids. Such accumulation of NDPK-B would amplify its effects in functional platform formation and protein recruitment at the membrane.

Original languageEnglish (US)
Pages (from-to)12923-12933
Number of pages11
JournalLangmuir
Volume32
Issue number48
DOIs
StatePublished - Dec 6 2016
Externally publishedYes

ASJC Scopus subject areas

  • General Materials Science
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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