Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Neuroscience
Link
http://www.nature.com/articles/nrn2276.pdf
Reference154 articles.
1. Matunis, M. J., Coutavas, E. & Blobel, G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135, 1457–1470 (1996).
2. Mahajan, R., Delphin, C., Guan, T., Gerace, L. & Melchior, F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97–107 (1997). Together with reference 1, this was the first study to identify SUMO1 as a covalent modifier protein. Both papers describe the role of SUMO in regulating the nuclear-pore localization of RanGAP.
3. Hayashi, T. et al. Ubc9 is essential for viability of higher eukaryotic cells. Exp. Cell Res. 280, 212–221 (2002).
4. Johnson, E. S. & Blobel, G. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem. 272, 26799–26802 (1997). This study, along with reference 137, indicated that the post-translational modification of proteins by SUMO in yeast and mammalian cells is mediated by UBC9, which is SUMO-specific and does not conjugate ubiquitin.
5. Tanaka, K. et al. Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell Biol. 19, 8660–8672 (1999).
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