Ubiquitination of Integral Membrane Proteins and Proteins in the Secretory Pathway
作者： Ron R. Kopito
DOI: 10.1007/978-1-4899-1922-9_13
关键词: Proteasome complex 、 F-box protein 、 Ubiquitin 、 Integral membrane protein 、 Cell biology 、 Peripheral membrane protein 、 Signal peptide 、 Chemistry 、 Secretory pathway 、 Golgi apparatus
摘要: Covalent modification of cellular proteins with ubiquitin represents a versatile intracellular signaling pathway that is linked to such diverse phenomena as DNA repair, organelle biogenesis, and protein turnover. Best understood among these the role system in targeting cytoplasmic for proteolysis by 26 S proteasome complex (reviewed Chapter 6). Although most substrates conjugation studied date have been or nuclear proteins, this chapter reviews recent data suggest degradation trafficking within central vacuolar system. By system, I refer collectively compartments secretory endocytic/lysosomal pathways including endoplasmic reticulum, Golgi apparatus, plasma membrane, lysosomes, various transitional transport vesicles.
springer.com
sci-hub.st 参考文章(94)
Y. Yarden, J. A. Escobedo, W-J. Kuang, T. L. Yang-Feng, T. O. Daniel, P. M. Tremble, E. Y. Chen, M. E. Ando, R. N. Harkins, U. Francke, V. A. Fried, A. Ullrich, L. T. Williams, Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors Nature. ,vol. 323, pp. 226- 232 ,(1986) , 10.1038/323226A0
John J.M. Bergeron, Michael B. Brenner, David Y. Thomas, David B. Williams, Calnexin: a membrane-bound chaperone of the endoplasmic reticulum Trends in Biochemical Sciences. ,vol. 19, pp. 124- 128 ,(1994) , 10.1016/0968-0004(94)90205-4
Dirk Görlich, Enno Hartmann, Siegfried Prehn, Tom A. Rapoport, A protein of the endoplasmic reticulum involved early in polypeptide translocation Nature. ,vol. 357, pp. 47- 52 ,(1992) , 10.1038/357047A0
Tadashi Suzuki, Ken Kitajima, Sadako Inoue, Yasuo Inoue, Occurrence and biological roles of ‘proximal glycanases’ in animal cells Glycobiology. ,vol. 4, pp. 777- 789 ,(1994) , 10.1093/GLYCOB/4.6.777
J Lowe, D Stock, B Jap, P Zwickl, W Baumeister, R Huber, Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science. ,vol. 268, pp. 533- 539 ,(1995) , 10.1126/SCIENCE.7725097
Duane D. Jenness, Phyllis Spatrick, Down regulation of the α-factor pheromone receptor in S. cerevisiae Cell. ,vol. 46, pp. 345- 353 ,(1986) , 10.1016/0092-8674(86)90655-0
Seng H. Cheng, Richard J. Gregory, John Marshall, Sucharita Paul, David W. Souza, Gary A. White, Catherine R. O'Riordan, Alan E. Smith, Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis Cell. ,vol. 63, pp. 827- 834 ,(1990) , 10.1016/0092-8674(90)90148-8
Emmanuel J. H. J. Wiertz, Domenico Tortorella, Matthew Bogyo, Joyce Yu, Walther Mothes, Thomas R. Jones, Tom A. Rapoport, Hidde L. Ploegh, Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. ,vol. 384, pp. 432- 438 ,(1996) , 10.1038/384432A0
Jennifer Lippincott-Schwartz, Juan S Bonifacino, Lydia C Yuan, Richard D Klausner, Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell. ,vol. 54, pp. 209- 220 ,(1988) , 10.1016/0092-8674(88)90553-3
E. D. Werner, J. L. Brodsky, A. A. McCracken, Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate Proceedings of the National Academy of Sciences of the United States of America. ,vol. 93, pp. 13797- 13801 ,(1996) , 10.1073/PNAS.93.24.13797