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Article

Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis

1
Instituto de Biotecnología, Universidad del Papaloapan, Tuxtepec 68301, Mexico
2
Departamento de Biología Molecular de Plantas, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca 62250, Mexico
3
Biology Department, University of Puget Sound, Tacoma, WA 98416, USA
4
Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06511, USA
*
Author to whom correspondence should be addressed.
Academic Editors: Ewa Muszyńska, Kinga Dziurka and Mateusz Labudda
Plants 2021, 10(10), 2228; https://doi.org/10.3390/plants10102228
Received: 16 September 2021 / Revised: 8 October 2021 / Accepted: 11 October 2021 / Published: 19 October 2021
SCF-type E3 ubiquitin ligases provide specificity to numerous selective protein degradation events in plants, including those that enable survival under environmental stress. SCF complexes use F-box (FBX) proteins as interchangeable substrate adaptors to recruit protein targets for ubiquitylation. FBX proteins almost universally have structure with two domains: A conserved N-terminal F-box domain interacts with a SKP protein and connects the FBX protein to the core SCF complex, while a C-terminal domain interacts with the protein target and facilitates recruitment. The F-BOX STRESS INDUCED (FBS) subfamily of plant FBX proteins has an atypical structure, however, with a centrally located F-box domain and additional conserved regions at both the N- and C-termini. FBS proteins have been linked to environmental stress networks, but no ubiquitylation target(s) or biological function has been established for this subfamily. We have identified two WD40 repeat-like proteins in Arabidopsis that are highly conserved in plants and interact with FBS proteins, which we have named FBS INTERACTING PROTEINs (FBIPs). FBIPs interact exclusively with the N-terminus of FBS proteins, and this interaction occurs in the nucleus. FBS1 destabilizes FBIP1, consistent with FBIPs being ubiquitylation targets SCFFBS1 complexes. This work indicates that FBS proteins may function in stress-responsive nuclear events, and it identifies two WD40 repeat-like proteins as new tools with which to probe how an atypical SCF complex, SCFFBS, functions via FBX protein N-terminal interaction events. View Full-Text
Keywords: F-box protein; SCF complex; stress response; WD40 repeat-like protein F-box protein; SCF complex; stress response; WD40 repeat-like protein
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MDPI and ACS Style

Sepulveda-Garcia, E.; Fulton, E.C.; Parlan, E.V.; O’Connor, L.E.; Fleming, A.A.; Replogle, A.J.; Rocha-Sosa, M.; Gendron, J.M.; Thines, B. Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis. Plants 2021, 10, 2228. https://doi.org/10.3390/plants10102228

AMA Style

Sepulveda-Garcia E, Fulton EC, Parlan EV, O’Connor LE, Fleming AA, Replogle AJ, Rocha-Sosa M, Gendron JM, Thines B. Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis. Plants. 2021; 10(10):2228. https://doi.org/10.3390/plants10102228

Chicago/Turabian Style

Sepulveda-Garcia, Edgar, Elena C. Fulton, Emily V. Parlan, Lily E. O’Connor, Anneke A. Fleming, Amy J. Replogle, Mario Rocha-Sosa, Joshua M. Gendron, and Bryan Thines. 2021. "Unique N-Terminal Interactions Connect F-BOX STRESS INDUCED (FBS) Proteins to a WD40 Repeat-like Protein Pathway in Arabidopsis" Plants 10, no. 10: 2228. https://doi.org/10.3390/plants10102228

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