Processing and activation of SUMO

Stable Identifier
Homo sapiens
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The initial translation products of SUMO1, SUMO2, and SUMO3 are precursors that have extra amino acid residues at the C-terminus (reviewed in Wang and Dasso 2009, Wilkinson and Henley 2010, Hannoun et al. 2010, Gareau and Lima 2010, Hay 2007). SUMO1 has 4 extra residues, SUMO2 has 2 extra residues, and SUMO3 has 11 extra residues. Proteolytic cleavage by SUMO peptidases (SENPs) removes the propeptide and leaves diglycine residues at the C-terminus. Each SENP has distinct preferences for certain SUMOs. SENP1 has highest activity on SUMO1; SENP2 and SENP5 have highest activity on SUMO2 (Shen et al. 2006, Reverter and Lima 2006, Mikolajczyk et al. 2007). SENP1 and SENP2 are predominantly nucleoplasmic (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006) and SENP5 is predominantly nucleolar (Di Bacco et al. 2006, Gong and Yeh 2006), therefore the processing reactions are believed to occur in the nucleus. The processed SUMO is then activated by formation of a thioester bond with a cysteine residue of an E1 enzyme, UBA2 (SAE2) in a complex with SAE1. SUMO is then transferred from the E1 enzyme to an E2 enzyme, UBC9 (UBE2I).
Literature References
PubMed ID Title Journal Year
20674646 Post-translational modification by SUMO

Hay, RT, Hannoun, Z, Jaffray, E, Greenhough, S, Hay, DC

Toxicology 2010
16738315 The SUMO-specific protease SENP5 is required for cell division

Ploegh, H, Catic, A, Gill, G, Lee, HY, Ouyang, J, Di Bacco, A

Mol. Cell. Biol. 2006
16253240 Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1

Lee, SJ, Kim, Y, Sung, KS, Choi, CY, Kim, YO, Kim, YH

FEBS Lett. 2005
16738331 Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2

Yeh, ET, Zhang, Y, Itahana, Y

Mol. Cell. Biol. 2006
20462400 Mechanisms, regulation and consequences of protein SUMOylation

Henley, JM, Wilkinson, KA

Biochem. J. 2010
11896061 Association of the human SUMO-1 protease SENP2 with the nuclear pore

Dasso, M, Hang, J

J. Biol. Chem. 2002
17099698 SUMO protease SENP1 induces isomerization of the scissile peptide bond

Tatham, MH, Naismith, JH, Shen, L, Hay, RT, Zagórska, A, Dong, C

Nat. Struct. Mol. Biol. 2006
21102611 The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition

Gareau, JR, Lima, CD

Nat. Rev. Mol. Cell Biol. 2010
17591783 Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs

Békés, M, Drag, M, Ronai, Z, Cao, JT, Mikolajczyk, J, Salvesen, GS

J. Biol. Chem. 2007
17099700 Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates

Reverter, D, Lima, CD

Nat. Struct. Mol. Biol. 2006
14563852 Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1

O'Hare, P, Bailey, D

J. Biol. Chem. 2004
17768054 SUMO-specific proteases: a twist in the tail

Hay, RT

Trends Cell Biol. 2007
12192048 Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex

Zhang, H, Matunis, MJ, Saitoh, H

Mol. Cell. Biol. 2002
19923268 SUMOylation and deSUMOylation at a glance

Dasso, M, Wang, Y

J. Cell. Sci. 2009
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