TY - JOUR
T1 - Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
AU - Bernier-Villamor, Victor
AU - Sampson, Deborah A.
AU - Matunis, Michael J.
AU - Lima, Christopher D.
N1 - Funding Information:
We thank John Buglino, Vincent Shen, and David R. Lima for technical assistance and the staff of beamline X4A at the National Synchrotron Light Source, a DOE facility. Beamline X4A is supported by the Howard Hughes Medical Institute. M.J.M. and D.A.S. are supported by a grant from the National Institutes of Health (GM60980). V.B.V. acknowledges support from the Secretarı́a de Estado de Educación y Universidades of Spain. C.D.L. acknowledges support from the Arnold and Mabel Beckman Foundation.
PY - 2002
Y1 - 2002
N2 - E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or through E3-mediated reactions. The small ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle progression in yeast. In contrast to most ubiquitin conjugation, the SUMO E2 enzyme Ubc9 is sufficient for substrate recognition and lysine modification of known SUMO targets. Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 Å reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins. Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IκBα, and RanGAP1.
AB - E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or through E3-mediated reactions. The small ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle progression in yeast. In contrast to most ubiquitin conjugation, the SUMO E2 enzyme Ubc9 is sufficient for substrate recognition and lysine modification of known SUMO targets. Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 Å reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins. Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IκBα, and RanGAP1.
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U2 - 10.1016/S0092-8674(02)00630-X
DO - 10.1016/S0092-8674(02)00630-X
M3 - Article
C2 - 11853669
AN - SCOPUS:0036177128
VL - 108
SP - 345
EP - 356
JO - Cell
JF - Cell
SN - 0092-8674
IS - 3
ER -