Molecular characterization of direct interactions between MPP1 and flotillins.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
20 07 2021
20 07 2021
Historique:
received:
10
01
2021
accepted:
28
06
2021
entrez:
21
7
2021
pubmed:
22
7
2021
medline:
10
11
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 34285255
doi: 10.1038/s41598-021-93982-3
pii: 10.1038/s41598-021-93982-3
pmc: PMC8292550
doi:
Substances chimiques
Blood Proteins
0
MPP1 protein, human
0
Membrane Proteins
0
Recombinant Proteins
0
flotillins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
14751Informations de copyright
© 2021. The Author(s).
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