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Editorial
. 2021 Oct 11:12:767281.
doi: 10.3389/fpls.2021.767281. eCollection 2021.

Editorial: Structure, Function, and Evolution of E3 Ligases and Targets

Derek J Gingerich  1 , Hanjo Hellmann  2 , Matthew J Christians  3 , Sophia L Stone  4
Affiliations
Editorial

Editorial: Structure, Function, and Evolution of E3 Ligases and Targets

Derek J Gingerich et al. Front Plant Sci. .
No abstract available

Keywords: E3 Ub-ligase; E3-ligases; ubiquitin (Ub); ubiquitin 26S-proteasome system; ubiquitin-like proteins (UBLs); ubiquitylation (Ubiquitination).

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Subunit composition of E3-ligases in plants. The numbers displayed within each subunit indicate the number of genes in the Arabidopsis thaliana genome putatively encoding the E3 ligase or E3 ligase component. (A) Schematics of E3 ubiquitin (Ub)-ligases in plants. RING (Really-Interesting New Gene) and U-box E3 ligases bind an E2 and the target and facilitate direct transfer of Ub to the target protein. HECT (Homologous to the E6AP Carboxyl Terminus) and RBR (RING-in-Between-RING) E3 ligases transfer the Ub from the E2 to a cysteine residue in the E3, then from the cysteine to the target protein. The CRLs (Cullin-RING Ligases) are multi-subunit structures with a Cullin (CUL) backbone protein that binds the E2 and a target adapter protein/complex. In SCF (Skp1/CUL1/F-box) complexes target adaptor F-box proteins bind to an Skp1 (S-phase Kinase-associated Protein 1)-like protein which interacts with CUL1. In the CRL3 complexes, a BTB (Broad-Complex, Tramtrack, and Bric-à-Brac) domain-containing protein binds to the target and CUL3. In the CRL4 complexes, WD40 domain-containing DWD (DDB1 Binding WD40) proteins bind the targets and interact with CUL4 through a DDB1 (Damaged DNA Binding 1) protein bridge. The APC/C (Anaphase-Promoting Complex/Cyclosome) contains at least 11 subunits. APC2 is a Cullin-like protein and APC11 is similar to RBX1 (Ring Box Protein 1). Target recognition occurs via the CDC20 (Cell Division Cycle 20), CDH1 (CDC20 Homolog 1), and APC10 subunits (Gray et al., ; Lechner et al., ; Schroeder et al., ; Capron et al., ; Downes et al., ; Gingerich et al., ; Stone et al., ; Kong et al., ; Lee et al., ; Lima et al., ; Marín, ; Trujillo, ; Saleme et al., 2021). (B) Schematic of the SUMO (Small Ub-like Modifier) E3-ligases. While SUMO E2s can directly interact with target proteins, the E3-ligases stimulate SUMO discharge by the E2 (Augustine and Vierstra, 2018) (https://www.frontiersin.org/articles/10.3389/fpls.2021.652170/full). (C) Proteins involved in the neddylation of Cullins. RBX1 functions synergistically with DCN1 (Defective in Cullin Neddylation 1) to facilitate the transfer of RUB (Related to Ubiquitin)/Nedd8 from the E2 RCE1 (RUB-Conjugating Enzyme 1) to Cullins. There are three possible homologs of DCN1 in Arabidopsis, though two lack the UBA (Ubiquitin-Associated) domain seen in other DCN1 proteins (Merlet et al., ; Hosp et al., 2014). (D) Schematic of the ATG8 (Autophagy-Related 8)/ATG12 conjugation pathway. The UBL ATG12 forms a thioester linkage with the E2 enzyme ATG10 and then is conjugated to ATG5. The UBL ATG8 is transferred to the E2 enzyme ATG3, then the ATG5-ATG12 conjugate, together with ATG16, acts as an E3 facilitating ATG8-phosphatidylethanolamine (PE) conjugation (Doelling et al., ; Bassham et al., ; Mizushima, 2020). (E) UFM1 (Ubiquitin-Fold Modifier 1) conjugation. UFL1 (UFM1-Specific Ligase 1) is the E3-ligase for UFM1 and catalyzes the UFMylation of multiple substrates. UFL1 ligase activity requires interaction with an adaptor protein called DDRGK1 (DDRGK Domain-Containing Protein 1). Another UFL1 interactor, CDK5RAP3 (CDK5 Regulatory Subunit-Associated Protein 3), affects the UFMylation profile and may serve as a substrate adaptor. DDRGK1 and CDK5RAP3 homologs are present in Arabidopsis; the CDK5RAP3 homolog is called C53 (Daniel and Liebau, ; Stephani et al., ; Witting and Mulder, 2021).
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  • Editorial on the Research Topic Structure, Function, and Evolution of E3 Ligases and Targets

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