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Review
. 2020 Apr 29;48(2):463-478.
doi: 10.1042/BST20190390.

The role of SUMOylation during development

Ana Talamillo  1 , Orhi Barroso-Gomila  1 , Immacolata Giordano  1 , Leiore Ajuria  1 , Marco Grillo  2   3 , Ugo Mayor  4   5 , Rosa Barrio  1
Affiliations
Review

The role of SUMOylation during development

Ana Talamillo et al. Biochem Soc Trans. .

Abstract

During the development of multicellular organisms, transcriptional regulation plays an important role in the control of cell growth, differentiation and morphogenesis. SUMOylation is a reversible post-translational process involved in transcriptional regulation through the modification of transcription factors and through chromatin remodelling (either modifying chromatin remodelers or acting as a 'molecular glue' by promoting recruitment of chromatin regulators). SUMO modification results in changes in the activity, stability, interactions or localization of its substrates, which affects cellular processes such as cell cycle progression, DNA maintenance and repair or nucleocytoplasmic transport. This review focuses on the role of SUMO machinery and the modification of target proteins during embryonic development and organogenesis of animals, from invertebrates to mammals.

Keywords: SUMO; development; ubiquitin.

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Conflict of interest statement

The authors declare that there are no competing interests associated with the manuscript.

Figures

Figure 1.
Figure 1.. The SUMOylation/deSUMOylation cycle.
(1) First, SENPs process newly synthesized SUMO precursor into mature SUMO. (2) Then, SUMO's exposed di-glycine forms a thioester bond with the SAE2's catalytic cysteine in an ATP-dependent manner. (3) SUMO is then passed from the SAE1/SAE2 E1 activating heterodimer to the E2 conjugating enzyme UBC9, which also forms a thioester bond. (4) Substrates can be directly modified by E2-SUMO, but E3s might enhance conjugation rates by binding either E2-SUMO or substrates. (5) SENPs cleave the isopeptide bond and SUMO as well as the substrate are recycled. S: SUMO. ∼: thioester bond.
See this image and copyright information in PMC

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