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Figures
- Fig. 1.
Protein ubiquitylation complexity. (A) The different steps in protein ubiquitylation through E1, E2 and E3 ligases are depicted. Ubiquitin (Ub) is transferred from the E1 to E2 and subsequently the HECT or RING E3 ligase. The E3 ligase interacts with the substrate for final ubiquitin transfer, either directly to the substrate acceptor site or to a lysine residue in already linked ubiquitin, resulting in chain formation. (B) A selection of different ubiquitin chain elongation and branching products are depicted with their associated cellular responses (e.g. proteasomal degradation or endocytosis) indicated. Importantly, the orientation of ubiquitin moieties is different in K48-linked chains compared to K63-linked chains. This allows different binding partners to associate to either of these poly-ubiquitin chains for signal transmission. Please note that additional linkage types are known, see also main text.
- Fig. 2.
Ubiquitin E3 ligases and DUBs regulating Rho GTPases. Indicated here are the different ubiquitin ligases as well as several identified DUBs that target the Rho GTPases. Barrier-protecting or -disrupting functions of the different Rho GTPases are highlighted, with RhoA and RhoB being disruptive, and Rac1 and Cdc42 protective. The Ras-like GTPase Rap1 is known for its barrier-stabilizing properties and is therefore included in the figure. See main text for further details. BACURD, BTB-containing adaptor for Cul3-mediated RhoA degradation.
- Fig. 3.
Ubiquitylation in cell–cell contacts. Overview of the various ubiquitin E3 ligases (in red) and DUBs (in green) that regulate junctional proteins in endothelial cells. In tight junctions, occludin and claudin-5 are regulated by the E3 ligases Itch and HECTD1, respectively, while ZO-1 is regulated by Ubr1. For adherens junctions, several other E3 ligases and their substrates, including both adhesion molecules and cell surface receptors, have been identified. The indicated ligases and DUBs that control endothelial integrity are discussed in more detail in the main text (see also Table 1).
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Article navigation
- Top
- Article
- ABSTRACT
- Introduction
- Ubiquitylation in cytokine-induced inflammation and vascular integrity
- Rho GTPase ubiquitylation and endothelial integrity
- Ubiquitin modifications at endothelial cell–cell junctions
- Ubiquitin ligases and junctional regulation
- Ubiquitin-dependent modifications in vascular disease
- Concluding remarks
- Footnotes
- References
- Figures & tables
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