title: SP-RING for SUMO: new functions bloom for a ubiquitin-like protein.
abstract: SUMO is covalently linked to a variety of cellular proteins. Three groups now describe related E3-like factors that enhance transfer of SUMO to specific proteins. This family of factors includes proteins important for chromosome condensation, signal transduction, and ion channel biogenesis.
authors.affiliation: Yale University, Department of Molecular Biophysics and Biochemistry, 266 Whitney Avenue, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu
authors.forename: M
authors.initials: M
authors.lastname: Hochstrasser
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D005656:Fungal Proteins / Q000378:metabolism; D020690:GTPase-Activating Proteins / Q000378:metabolism; D006801:Humans; D008025:Ligases; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D025842:SUMO-1 Protein / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D044767:Ubiquitin-Protein Ligases
chemical_list: D005656:Fungal Proteins; D020690:GTPase-Activating Proteins; C092317:RANGAP1 protein, human; D025842:SUMO-1 Protein; D029701:Saccharomyces cerevisiae Proteins; C436836:Siz2 protein, S cerevisiae; D044767:Ubiquitin-Protein Ligases; D008025:Ligases; C436837:Siz1 protein, S cerevisiae