@article{Ukleja:2024:10.1038/s41467-024-49951-1,
author = {Ukleja, M and Kricks, L and Torrens, G and Peschiera, I and Rodrigues-Lopes, I and Krupka, M and García-Fernández, J and Melero, R and del, Campo R and Eulalio, A and Mateus, A and López-Bravo, M and Rico, AI and Cava, F and Lopez, D},
doi = {10.1038/s41467-024-49951-1},
journal = {Nature Communications},
title = {Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains},
url = {http://dx.doi.org/10.1038/s41467-024-49951-1},
volume = {15},
year = {2024}
}

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TY  - JOUR
AB  - <jats:title>Abstract</jats:title><jats:p>The function of many bacterial processes depends on the formation of functional membrane microdomains (FMMs), which resemble the lipid rafts of eukaryotic cells. However, the mechanism and the biological function of these membrane microdomains remain unclear. Here, we show that FMMs in the pathogen methicillin-resistant <jats:italic>Staphylococcus aureus</jats:italic> (MRSA) are dedicated to confining and stabilizing proteins unfolded due to cellular stress. The FMM scaffold protein flotillin forms a clamp-shaped oligomer that holds unfolded proteins, stabilizing them and favoring their correct folding. This process does not impose a direct energy cost on the cell and is crucial to survival of ATP-depleted bacteria, and thus to pathogenesis. Consequently, FMM disassembling causes the accumulation of unfolded proteins, which compromise MRSA viability during infection and cause penicillin re-sensitization due to PBP2a unfolding. Thus, our results indicate that FMMs mediate ATP-independent stabilization of unfolded proteins, which is essential for bacterial viability during infection.</jats:p>
AU  - Ukleja,M
AU  - Kricks,L
AU  - Torrens,G
AU  - Peschiera,I
AU  - Rodrigues-Lopes,I
AU  - Krupka,M
AU  - García-Fernández,J
AU  - Melero,R
AU  - del,Campo R
AU  - Eulalio,A
AU  - Mateus,A
AU  - López-Bravo,M
AU  - Rico,AI
AU  - Cava,F
AU  - Lopez,D
DO  - 10.1038/s41467-024-49951-1
PY  - 2024///
TI  - Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-024-49951-1
VL  - 15
ER  - 

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