SCF Ligases and Their Functions in Oogenesis and Embryogenesis—Summary of the Most Important Findings throughout the Animal Kingdom

Abstract

SCF-dependent proteolysis was first discovered via genetic screening of budding yeast almost 25 years ago. In recent years, more and more functions of SCF (Skp1-Cullin 1-F-box) ligases have been described, and we can expect the number of studies on this topic to increase. SCF ligases, which are E3 ubiquitin multi-protein enzymes, catalyse protein ubiquitination and thus allow protein degradation mediated by the 26S proteasome. They play a crucial role in the degradation of cell cycle regulators, regulation of the DNA repair and centrosome cycle and play an important role in several diseases. SCF ligases seem to be needed during all phases of development, from oocyte formation through fertilization, activation of the embryonic genome to embryo implantation. In this review, we summarize known data on SCF ligase-mediated degradation during oogenesis and embryogenesis. In particular, SCFβTrCP and SCFSEL-10/FBXW7 are among the most important and best researched ligases during early development. SCFβTrCP is crucial for the oogenesis of Xenopus and mouse and also in Xenopus and Drosophila embryogenesis. SCFSEL-10/FBXW7 participates in the degradation of several RNA-binding proteins and thereby affects the regulation of gene expression during the meiosis of C. elegans. Nevertheless, a large number of SCF ligases that are primarily involved in embryogenesis remain to be elucidated.

FBXO11 amplifies type I interferon signaling to exert antiviral effects by facilitating the assemble of TRAF3–TBK1–IRF3 complex

“…A pivotal E3‐Ub ligase SKP/Cullin/F‐box (SCF) complex has been shown to regulate protein interactions, functionalization, and localization by various patterns of ubiquitination 9,10 . Specific protein substrates targeted for ubiquitination via the SCF complex are recognized by multiple F‐box family proteins 11,12 . Then F‐box proteins further enhance the interaction with SKP1, which in turn binds to CUL1 and RBX1 to activate E2 Ub ligase 9 .…”

“…9,10 Specific protein substrates targeted for ubiquitination via the SCF complex are recognized by multiple F-box family proteins. 11,12 Then F-box proteins further enhance the interaction with SKP1, which in turn binds to CUL1 and RBX1 to activate E2 Ub ligase. 9 Several lysine residues, including K48 and K11, are critical for the proteasomal degradation of substrate proteins via the SCF complex, whereas K63 primarily plays a signal transduction role for protein interactions.…”

The association of the expression of RBX1 and BAMBI in polycystic ovarian syndrome patients' cumulus cells and oocyte maturation

“…The catalytic core of SCF, a multi-subunit proteasome, is formed by RBX1, one of its essential constituents (10). Indirect activation of APC/Cdc20 by RBX1 can cause an oocyte to bypass the GV stage and advance to the MII stage (11,12). This study aimed to determine if these genes are involved in the etiology of PCOS or oocyte maturation, taking into account their role in ovulation.…”