ArticleScientific reports2021
Molecular characterization of direct interactions between MPP1 and flotillins.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- The Arabidopsis SPFH protein HIR2 modulates receptor signaling and plasma membrane organization.The EMBO journal · 2026Article
- Review
- Flotillins in membrane trafficking and physiopathology.Biology of the cell · 2025Review
- Structure of the flotillin complex in a native membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- EFR3A: a new raft domain organizing protein?Cellular & molecular biology letters · 2023Article
- ABCA1 transporter promotes the motility of human melanoma cells by modulating their plasma membrane organization.Biological research · 2023Article
- MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules.Cells · 2022Article
- Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flotillins are the major structural proteins in erythroid raft domains. We have shown previously that the dynamic nanoscale organization of raft domains in erythroid cells may depend on flotillin-MPP1 interactions. Here, by using molecular dynamic simulations and a surface plasmon resonance-based approach we determined that high-affinity complexes of MPP1 and flotillins are formed via a so far unidentified region within the D5 domain of MPP1. Significantly, this particular "flotillin binding motif" is of key physiological importance, as overexpression of peptides containing this motif inhibited endogenous MPP1-flotillin interaction in erythroid precursor cells, thereby causing lateral disorganization of raft domains. This was reflected by both reduction in the plasma membrane order and markedly decreased activation of signal transduction via the raft-dependent insulin receptor pathway. Our data highlight new molecular details concerning the mechanism whereby MPP1 functionally links flotillins to exert their physiological role in raft domain formation.
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