HSP90 differentially stabilizes plant ABCB-type auxin transporters on the plasma membrane
Jazyk angličtina Země Anglie, Velká Británie Médium electronic
Typ dokumentu časopisecké články
Grantová podpora
31003A_165877
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation)
310030_197563
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation)
PubMed
41027915
PubMed Central
PMC12484997
DOI
10.1038/s41467-025-63780-w
PII: 10.1038/s41467-025-63780-w
Knihovny.cz E-zdroje
- MeSH
- ABC transportéry * metabolismus genetika MeSH
- Arabidopsis * metabolismus genetika MeSH
- biologický transport MeSH
- buněčná membrána * metabolismus MeSH
- kyseliny indoloctové * metabolismus MeSH
- P-glykoproteiny * metabolismus genetika MeSH
- protein - isoformy metabolismus MeSH
- proteiny huseníčku * metabolismus genetika MeSH
- proteiny tepelného šoku HSP90 * metabolismus genetika MeSH
- proteiny vázající takrolimus metabolismus genetika MeSH
- rostlinné proteiny metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- ABC transportéry * MeSH
- kyseliny indoloctové * MeSH
- P-glykoproteiny * MeSH
- protein - isoformy MeSH
- proteiny huseníčku * MeSH
- proteiny tepelného šoku HSP90 * MeSH
- proteiny vázající takrolimus MeSH
- rostlinné proteiny MeSH
Closely related FKBP orthologs, FKBP42/TWISTED DWARF1 (TWD1) and FKBP38, have been shown to control the biogenesis of plant and mammalian ATP-binding cassette (ABC) transporters, respectively. However, the mechanistic role of the described FKBP-ABCB interaction is widely unknown. Here, we verify cytosolic HEAT-SHOCK PROTEIN90 (HSP90) isoforms as valid interactors of TWD1 and map HSP90 binding to an amphiphilic alpha-helix preceding its TPR domain. We provide pharmacological and genetic evidence that a subset of TWD1-interacting ABCBs, in contrast to mammalian ABCBs, are constitutive HSP90 clients in plants. This effect and its specificity are presumably provided by TWD1. Our data strongly correlate the impact of HSP90 inhibition on ABCB-mediated development and ABCB plasma membrane stability on the one hand and ABCB cycling rate on the other. In summary, we uncover a dynamic mechanism of HSP90 for differential stabilization of the plasma membrane ABCB isoforms to regulate polar auxin transport and to confer developmental plasticity.
Department of Plant and Microbial Biology University of Zürich Zürich Switzerland
LINV DIPSAA Università di Firenze Florence Italy
Mendel Centre for Plant Genomics and Proteomics Masaryk University CEITEC MU Brno Czech Republic
Technische Universität Dresden Faculty of Biology Dresden Germany
University of Fribourg Department of Biology Fribourg Switzerland
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