Plant F-box Proteins – Judges between Life and Death

• Published in: Critical reviews in plant sciences Vol. 34; no. 6; pp. 523 - 552
• Main Authors: Stefanowicz, Karolina, Lannoo, Nausicaä, Van Damme, Els J.M
• Format: Journal Article
• Language: English
• Published: Boca Raton Taylor & Francis 02-11-2015; Taylor & Francis Ltd
• Subjects: 26S proteasome; carbohydrate binding; Carbohydrates; Control systems; death; Defense mechanisms; Degradation; Enzymes; Eukaryotes; eukaryotic cells; F-box protein; F-box proteins; Flowers & plants; glycan; Glycoprotein; glycoproteins; growth and development; Hormones; lectin; Nictaba; plant development; plant growth; proteasome endopeptidase complex; protein degradation; Proteins; Recognition; regulatory proteins; SCF complex; ubiquitin; ubiquitination; UPS
• ISSN: 1549-7836; 0735-2689; 1549-7836
• DOI: 10.1080/07352689.2015.1024566

Selective protein degradation through the ubiquitin–26S proteasome system is a key mechanism for post-translational control of regulatory proteins in all eukaryotes. The pivotal components in this system are the multi-subunit E3 Ub-ligase enzymes responsible for specific recognition and ubiquitination of degradation targets. In this review, we focus on plant F-box proteins which confer specificity to the SCF-type E3 enzyme complexes. F-box proteins represent one of the largest and most heterogeneous superfamilies in plants, with hundreds of different representatives exposing an extensive variability of C-terminal target-binding domains, and as such, modulating almost every aspect of plant growth and development. Since the first reports on plant F-box proteins over a decade ago, a lot of progress has been made in our understanding of their relevance for plant physiology. In this review, we combine well-established knowledge with the most recent advances related to plant F-box proteins and their role in plant development, hormone signaling and defense pathways. We also elaborate on the yet poorly described carbohydrate-binding plant F-box proteins presumably targeting glycoproteins for proteasomal degradation.