HSP90 differentially stabilizes plant ABCB-type auxin transporters on the plasma membrane

. 2025 Sep 30 ; 16 (1) : 8643. [epub] 20250930

Jazyk angličtina Země Anglie, Velká Británie Médium electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid41027915

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)

Odkazy

PubMed 41027915
PubMed Central PMC12484997
DOI 10.1038/s41467-025-63780-w
PII: 10.1038/s41467-025-63780-w
Knihovny.cz E-zdroje

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.

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