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Molecular characterization of direct interactions between MPP1 and flotillins

التفاصيل البيبلوغرافية
العنوان: Molecular characterization of direct interactions between MPP1 and flotillins
المؤلفون: Agnieszka Biernatowska, Paulina Olszewska, Krzysztof Grzymajło, Dominik Drabik, Sebastian Kraszewski, Aleksander F. Sikorski, Aleksander Czogalla
المصدر: Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
بيانات النشر: Nature Portfolio, 2021.
سنة النشر: 2021
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2045-2322
Relation: https://doaj.org/toc/2045-2322
DOI: 10.1038/s41598-021-93982-3
URL الوصول: https://doaj.org/article/8e62c81e730642f4a790ff25c2654fee
رقم الأكسشن: edsdoj.8e62c81e730642f4a790ff25c2654fee
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20452322
DOI:10.1038/s41598-021-93982-3