Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation Export

@article{citeulike:4065646, abstract = {The ubiquitin-dependent targeting of proteins to the proteasome is an essential mechanism for regulating eukaryotic protein stability. Here we define the minimal signal for the degradation of the S phase CDK inhibitor Sic1. Of 20 lysines scattered throughout Sic1, 6 N-terminal lysines serve as major ubiquitination sites. Sic1 lacking these lysines (K0N) is stable in vivo, but readdition of any one restores turnover. Nevertheless, ubiquitin chains attached at different N-terminal lysines specify degradation in vitro at markedly different rates. Moreover, although K0N can be ubiquitinated by SCF Cdc4 /Cdc34 in vitro in the absence (but not in the presence) of S-CDK, it is degraded slowly. Our results reveal that a single multiubiquitin chain can sustain a physiological turnover rate, but that chain position plays an unexpectedly significant role in the rate of proteasomal proteolysis.}, author = {Petroski, M.}, citeulike-article-id = {4065646}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S1097-2765(03)00221-1}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S1097-2765(03)00221-1}, doi = {10.1016/S1097-2765(03)00221-1}, issn = {10972765}, journal = {Molecular Cell}, keywords = {degradation, scf, ubiquitin-pathway}, month = {June}, number = {6}, pages = {1435--1444}, posted-at = {2009-02-17 19:47:49}, priority = {0}, title = {Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation}, url = {http://dx.doi.org/10.1016/S1097-2765(03)00221-1}, volume = {11}, year = {2003} }

TY - JOUR ID - citeulike:4065646 L3 - citeulike-article-id:4065646 N2 - The ubiquitin-dependent targeting of proteins to the proteasome is an essential mechanism for regulating eukaryotic protein stability. Here we define the minimal signal for the degradation of the S phase CDK inhibitor Sic1. Of 20 lysines scattered throughout Sic1, 6 N-terminal lysines serve as major ubiquitination sites. Sic1 lacking these lysines (K0N) is stable in vivo, but readdition of any one restores turnover. Nevertheless, ubiquitin chains attached at different N-terminal lysines specify degradation in vitro at markedly different rates. Moreover, although K0N can be ubiquitinated by SCF Cdc4 /Cdc34 in vitro in the absence (but not in the presence) of S-CDK, it is degraded slowly. Our results reveal that a single multiubiquitin chain can sustain a physiological turnover rate, but that chain position plays an unexpectedly significant role in the rate of proteasomal proteolysis. IS - 6 JF - Molecular Cell SN - 10972765 EP - 1444 TI - Context of Multiubiquitin Chain Attachment Influences the Rate of Sic1 Degradation VL - 11 SP - 1435 KW - degradation KW - scf KW - ubiquitin-pathway AU - Petroski, M PY - 2003/06// UR - http://dx.doi.org/10.1016/S1097-2765(03)00221-1 ER -