核糖体自噬汇总.docxVIP

Downloaded from on December 17, 2015 - Published by Cold Spring Harbor Laboratory Press Downloaded from on December 17, 2015 - Published by Cold Spring Harbor Laboratory Press Downloaded from on December 17, 2015 - Published by Cold Spring Harbor Laboratory Press Downloaded from on December 17, 2015 - Published by Cold Spring Harbor Laboratory Press Both the autophagy and proteasomal pathways facilitate the Ubp3p-dependent depletion of a subset of translation and RNA turnover factors during nitrogen starvation in Saccharomyces cerevisiae SHANE P. KELLY1 and DAVID M. BEDWELL1,2 1 Department of Cell, Developmental and Integrative Biology, 2Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA ABSTRACT Protein turnover is an important regulatory mechanism that facilitates cellular adaptation to changing environmental conditions. Previous studies have shown that ribosome abundance is reduced during nitrogen starvation by a selective autophagy mechanism termed ribophagy, which is dependent upon the deubiquitinase Ubp3p. In this study, we asked whether the abundance of various translation and RNA turnover factors are reduced following the onset of nitrogen starvation in Saccharomyces cerevisiae. We found distinct differences in the abundance of the proteins tested following nitrogen starvation: (1) The level of some did not change; (2) others were reduced with kinetics similar to ribophagy, and (3) a few proteins were rapidly depleted. Furthermore, different pathways differentially degraded the various proteins upon nitrogen starvation. The translation factors eRF3 and eIF4GI, and the decapping enhancer Pat1p, required an intact autophagy pathway for their depletion. In contrast, the deadenylase subunit Pop2p and the decapping enzyme Dcp2p were rapidly depleted by a proteasome-dependent mechanism. The proteasome-dependent depletion of Dcp2p and Pop2p was also induced by rapamycin, suggesting that the TOR1 pathway influences th