The covalent attachment of a small ubiquitin-related modifier (SUMO) to substrate protein, a process that is biochemically analogous to, but functionally distinct from, ubiquitination; sumoylation is critical to many different biological processes—e.g., protein localisation and stability, transcriptional activities, nucleocytoplasmic signalling and transport, genome replication, and regulation of gene expression
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Our recent studies have addressed the molecular basis for transformation and demonstrated the essential role of sumoylation of the PML moiety of PML/RARA, relaxed DNA-binding specificity, binding to RXRA, for both transcriptional repression and transformation in primary cells, uncovering an unexpected level of complexity for in vivo transformation.
On the other hand, proteins which regulate the protein modification processes such as folding, sumoylation, ubiquitination and phosphatase activity also displayed significant alteration in the expression level upon intervention with MNQ.
The SUMOylation is a dynamic and reversible process regulated by both conjugation and de-conjugation enzymes via a three-step process and three enzyme reactions, E1 (SUMO-activation enzyme) (activation), E2 (SUMO conjugation enzyme) (conjugation), and E3 (SUMO ligase) (ligation).
Mapping the mitochondrial proteome, post-translational modifications (including phosphorylation, acetylation, sumoylation, parylation) in different cell types and stages of development, and combining mitochondrial proteome analysis with imaging will be informative, especially given the wide variability in mitochondrial form and function in different tissues and developmental stages (Johnson et al.
Histone modifications are varied and include acetylation, methylation, phosphorylation, ubiquitinylation, ADP-ribosylation, and sumoylation at specified residues (for a review, see Kouzarides 2007).
The SUMOylation influences stability, interaction, cellular localization, and activity of proteins and thereby regulates processes, such as DNA repair (Hoege et al.
In addition, post-translational modifications such as phosphorylation, SUMOylation and acetylation of specific residues in several polyQ proteins can be altered in the presence of the mutation, affecting interactions with their natural binding proteins.
Protein function is controlled by altering their structure in processes that can be independent or inter-related including phosphorylation, ubiquitination and SUMOylation.
Editor Ulrich (Clare Hall Laboratories, London Research Institute, Cancer Research UK) presents 20 papers that, following an overview of the SUMO system, discuss identification of SUMO targets, identification of SUMO interactions, functional analysis of sumoylation in vivo, biochemical studies of SUMO conjugation, biochemical studies of SUMO deconjugation, and manipulation and alternative uses of the SUMO system.
Modifications such as acetylation, phosphorylation, methylation, de-imination, ubiquitylation, sumoylation, ADP-ribosylation and proline isomerization generate diversity in histone structure.
The team suggests that clumping renders the mutant form of huntingtin harmless, but that sumoylation makes the protein soluble and thus toxic.
Small ubiquitin-related modifier (SUMO)-1, SUMO-2/3 and SUMOylation are involved with centromeric heterochromatin of chromosomes 9 and 1 and proteins of the synaptonemal complex during meiosis in men," Human Reproduction 23(12): 2850-2857.