Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8. Export

@article{citeulike:842997, abstract = {While proteasome is central to the degradation of cellular ubiquitinated proteins, the control of its nuclear function is barely understood. Here we show that the fission yeast ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1 are responsible for nuclear enrichment of proteasome through the function of Cut8, a nuclear envelope protein. Cut8 is an Rhp6 substrate that physically interacts with and tethers proteasome. Nonubiquitinatable K-all-R Cut8 weakly interacts with proteasome and fails to enrich nuclear proteasome. Consistently, the nuclear enrichment of proteasome also fails in rhp6 and ubr1 null mutants. Further, cut8 null and cut8 K-all-R mutants are hypersensitive to DNA damage, probably due to the paucity of nuclear proteasome. Thus, Rhp6 enhances the retention of nuclear proteasome through regulating Cut8. The short-lived nature of Cut8 is crucial for feedback enrichment of the proteasome within the nucleus. This is likely to be a conserved mechanism as we describe a Cut8 homolog in flies.}, address = {Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.}, author = {Takeda, K. and Yanagida, M.}, citeulike-article-id = {842997}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2005.05.023}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16096059}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16096059}, day = {12}, doi = {10.1016/j.cell.2005.05.023}, issn = {0092-8674}, journal = {Cell}, keywords = {cell, chromosome, cut8, cycle, proteasome}, month = {August}, number = {3}, pages = {393--405}, posted-at = {2006-09-14 09:30:56}, priority = {2}, title = {Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8.}, url = {http://dx.doi.org/10.1016/j.cell.2005.05.023}, volume = {122}, year = {2005} }

TY - JOUR ID - citeulike:842997 L3 - citeulike-article-id:842997 N2 - While proteasome is central to the degradation of cellular ubiquitinated proteins, the control of its nuclear function is barely understood. Here we show that the fission yeast ubiquitin-conjugating Rhp6/Ubc2/Rad6 and ligating enzymes Ubr1 are responsible for nuclear enrichment of proteasome through the function of Cut8, a nuclear envelope protein. Cut8 is an Rhp6 substrate that physically interacts with and tethers proteasome. Nonubiquitinatable K-all-R Cut8 weakly interacts with proteasome and fails to enrich nuclear proteasome. Consistently, the nuclear enrichment of proteasome also fails in rhp6 and ubr1 null mutants. Further, cut8 null and cut8 K-all-R mutants are hypersensitive to DNA damage, probably due to the paucity of nuclear proteasome. Thus, Rhp6 enhances the retention of nuclear proteasome through regulating Cut8. The short-lived nature of Cut8 is crucial for feedback enrichment of the proteasome within the nucleus. This is likely to be a conserved mechanism as we describe a Cut8 homolog in flies. IS - 3 JF - Cell SN - 0092-8674 AD - Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan. EP - 405 TI - Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8. VL - 122 SP - 393 KW - cell KW - chromosome KW - cut8 KW - cycle KW - proteasome AU - Takeda, K AU - Yanagida, M PY - 2005/08/12/ UR - http://dx.doi.org/10.1016/j.cell.2005.05.023 ER -