The N-end rule: functions, mysteries, uses.
- 29 October 1996
- journal article
- review article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 93 (22) , 12142-12149
- https://doi.org/10.1073/pnas.93.22.12142
Abstract
The N-end rule relates the in vivo half-life of a protein to the identity of its N-terminal residue. Similar but distinct versions of the N-end rule operate in all organisms examined, from mammals to fungi and bacteria. In eukaryotes, the N-end rule pathway is a part of the ubiquitin system. I discuss the mechanisms and functions of this pathway, and consider its applications.Keywords
This publication has 68 references indexed in Scilit:
- Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascadeNature, 1995
- A two-component system that regulates an osmosensing MAP kinase cascade in yeastNature, 1994
- Ubiquitin found in the archaebacterium Thermoplasma acidophilumFEBS Letters, 1993
- A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytesNature, 1992
- Mechanisms and Functions of Cell DeathAnnual Review of Cell Biology, 1991
- The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme.Proceedings of the National Academy of Sciences, 1991
- Independent inactivation of MPF and cytostatic factor (Mos) upon fertilization of Xenopus eggsNature, 1991
- Naming a targeting signalPublished by Elsevier ,1991
- Cis-trans recognition and subunit-specific degradation of short-lived proteinsNature, 1990
- The site of amino acid addition to postranslationally modified proteins of regenerating rat sciatic nervesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990