The nucleoporin RanBP2 has SUMO1 E3 ligase activity.

By A. Pichler, Andreas Gast, J. Seeler, A. Dejean, F. Melchior. Cell, 2002

850 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/42286566b08b8c1742c8477e6b242e006d8c3c02

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

1. G. Gill

In Molecular Biology

1. G. Gill
2. J. Seeler
3. A. Dejean
4. F. Melchior
5. C. Lima
6. Michael P. Rout
7. Brian T. Chait
8. Wenzhu Zhang

Citations in the corpus

• Sumoylation is involved in β‐catenin‐dependent activation of Tcf‐4 (2003, background): “…transferred to the E2 conjugation enzyme Ubc9, and ®nally conjugated to target proteins by either of the E3 ligases: protein inhibitor of activated STAT (PIAS) (Johnson et al., 1997; Saitoh et al., 1998; Kahyo et al., 2001; Sachdev et al., 2001) or RanBP2 (Kirsh et al., 2002; Pichler et al., 2002).”
• The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition (2010, background): “, and a family of SP-RING -containing proteins, including the Siz and protein inhibitor of STAT (PIAS) protein”
• Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “In vitro experiments have shown that high concentration of Ubc9 and the E1 enzy e is often sufficient to SUMOylate a substrate protein [98,99].”
• SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? (2004, background): “SUMO modification of RanGAP greatly increases its interaction with RanBP2 (also known as Nup358), a component of the nuclear pore complex and a SUMO E3 ligase (Pichler et al. 2002).”
• Proteomic analysis of the mammalian nuclear pore complex (2002, background): “In vertebrates, the SUMO E2 conjugating enzyme, Ubc9, and the E3 ligase, Nup358, also associate with NPCs (Saitoh et al., 1997; Pichler et al., 2002) although it is unknown if E2 or E3 enzymes associate with the yeast NPC.”
• Sumoylation: a regulatory protein modification in health and disease. (2013, background): “The SUMO E3 ligase RanBP2 forms chains with SUMO1 in vitro (67), and SUMO chains involving several lysines in SUMO1 (K7, -17, -25), SUMO2 (K32, -34), and SUMO3 (K33, -35) seem to exist in vivo, found by mass spectrometric analyses (116, 127–129).”
• Nuclear and unclear functions of SUMO (2003, background): “, and similar structures, using different lysine acceptor(s), might also be formed by SUMO1 (Ref”
• Concepts in sumoylation: a decade on (2007, background): “The vertebrate-specific nuclear pore protein RanBP2 represents a second type of SUMO E3 ligase”
• The nuclear pore complex and nuclear transport. (2010, background): “However, it also has a domain with E3 SUMO1 ligase activity and docks the sumolylation cofactor enzyme Ubc9 to facilitate the addition of SUMO to targets directly at the cytoplasmic filaments (Pichler et al. 2002; Reverter and Lima 2005).”