Abstract: SUMO modification is a reversible post-translational regulation of proteins. It resembles the three-dimensional structure of ubiquitin, but different functional outcomes derive from these two types of modification. It targets a variety of proteins within the nucleus, in the plasma membrane and cytoplasm of the cell. Numerous developmental proteins, including transcription factors and epigenetic regulators, have been identified as sumoylation substrates. It is covalently conjugated with specific lysine sites on target proteins through E1 activating enzymes, E2 binding enzymes and E3 ligase, and plays a regulatory role in cell function, such as controlling cell cycle, regulating transcription, regulating subcellular localization, etc. In recent years, several researches have uncovered many significant functions of the sumoylation in the early life of embryonic development. In the process of embryonic development, sumoylation involved in many molecular events in multiple aspects of the regulation of embryonic development, such as maintaining chromosome integrity and isolation, control of centromere aggregation and regulation of germ cell development and meiotic maturation etc. The review will generalize current information as to the function of sumoylation in the embryonic development. However, as the study has just been started, the full physiological function of the SUMO loop pathway in embryonic development remains to be further studied.

Key words: Ubiquitin, Embryonic development, Protein modification, translational, Small ubiquitin-related modifier