• Publications
  • Influence
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2Expand
  • 360
  • 38
  • PDF
Ube2W conjugates ubiquitin to α-amino groups of protein N-termini
The covalent attachment of the protein ubiquitin to intracellular proteins by a process known as ubiquitylation regulates almost all major cellular systems, predominantly by regulating proteinExpand
  • 77
  • 10
  • PDF
Structural basis for the RING catalyzed synthesis of K63 linked ubiquitin chains
RING E3 ligase–catalyzed formation of K63-linked ubiquitin chains by the Ube2V2–Ubc13 E2 complex is required in many important biological processes. Here we report the structure of the RING-domainExpand
  • 73
  • 10
  • PDF
Proteome-Wide Identification of SUMO2 Modification Sites
A novel method for the enrichment of SUMO2-modified peptides reveals more than 1000 sites of modification in human cells. Sleuthing SUMO Sites Covalent attachment to small ubiquitin-like modifiersExpand
  • 148
  • 7
  • PDF
SUMOylation of the GTPase Rac1 is required for optimal cell migration
The Rho-like GTPase, Rac1, induces cytoskeletal rearrangements required for cell migration. Rac activation is regulated through a number of mechanisms, including control of nucleotide exchange andExpand
  • 134
  • 7
  • PDF
Arsenic-Induced SUMO-Dependent Recruitment of RNF4 into PML Nuclear Bodies
Here we analyze the nuclear trafficking dynamics of PML and its SUMO-dependent ubiquitin ligase, RNF4, in response to arsenic. We show that arsenic induces rapid reorganization of the cell nucleus byExpand
  • 64
  • 5
  • PDF
The SUMO protease SENP6 is a direct regulator of PML nuclear bodies
We show that SUMO-specific protease SENP6 can cleave mixed SUMO-1 and SUMO-2/3 chains. Depletion of SENP6 results in accumulation of SUMO-2/3 and SUMO-1 conjugates in promyelocytic leukemia (PML)Expand
  • 53
  • 5
Characterization of SENP7, a SUMO-2/3-specific isopeptidase.
The modification of proteins by SUMO (small ubiquitin-related modifier) plays important roles in regulating the activity, stability and cellular localization of target proteins. Similar toExpand
  • 88
  • 4
  • PDF
Mechanism of ubiquitylation by dimeric RING ligase RNF4
Mammalian RNF4 is a dimeric RING ubiquitin E3 ligase that ubiquitylates poly-SUMOylated proteins. We found that RNF4 bound ubiquitin-charged UbcH5a tightly but free UbcH5a weakly. To provide insightExpand
  • 132
  • 3
  • PDF
SUMO Chain-Induced Dimerization Activates RNF4
Summary Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis. RNF4 is anExpand
  • 56
  • 3
  • PDF