Retrograde transport of tobacco phytaspase is mediated by its partner, Tubby-like F-box protein 8

Galiullina, R.A.; Pigidanov, A.A.; Safronov, G.G.; Trusova, S.V.; Teplova, A.D.; Golyshev, S.A.; Serebryakova, M.V.; Kovaleva, I.E.; Litvinova, A.V.; Chichkova, N.V.; Vartapetian, A.B.

Авторы: Galiullina R.A., Pigidanov A.A., Safronov G.G., Trusova S.V., Teplova A.D., Golyshev S.A., Serebryakova M.V., Kovaleva I.E., Litvinova A.V., Chichkova N.V., Vartapetian A.B.
Журнал: International Journal of Molecular Sciences
Том: 26
Год издания: 2025
Издательство: MDPI
Местоположение издательства: Basel, Switzerland
Номер статьи: 2236
DOI: 10.3390/ijms26052236
Аннотация: Phytaspases, plant cell death-promoting and proprotein-processing proteolyticenzymes of the plant subtilase family, display aspartate (caspase-like) cleavage specificityand a very unusual retrograde trafficking from the apoplast to the cell interior uponinduction of death-inducing stresses. To determine the underlying molecular mechanisms,we performed a search for tobacco phytaspase (NtPhyt) interactors using an in vivo crosslinkingapproach in Nicotiana tabacum plants. Tobacco Tubby-like F-box protein 8 (namedTubic hereafter) was identified as an NtPhyt interactor, with formation of the cross-linkedcomplex being only efficient under the oxidative stress conditions. Direct interaction ofthe two proteins was further corroborated in the in vitro experiments. Analysis of Tubic-EGFP behavior in plant cells revealed that Tubic is a membrane-associated and fairlyunstable protein. Furthermore, we showed that NtPhyt and Tubic are capable of negativelyaffecting one another in plant cells. On the other hand, down-regulation of Tubic in Tubicsilencedplants impaired specifically the retrograde transport of NtPhyt upon the inductionof oxidative stress, testifying to a critical role of Tubic in this process.
Добавил в систему: Вартапетян Андрей Борисович

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Retrograde transport of tobacco phytaspase is mediated by its partner, Tubby-like F-box protein 8статья

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