Cited by 859Ubiquitin and proteasome pathwaysAutophagy in Disease and TherapyProtein Structure and Dynamics

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The N-end rule: functions, mysteries, uses

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Varshavsky, A·1996·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.93.22.12142PMC PMC37957

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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.

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Authors: Varshavsky, A.
Affiliations: California Institute of Technology (US)
Corresponding author: Varshavsky, A
ORCID: Varshavsky, A
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1996-10-29
Volume: 93
Issue: 22
Pages: 12142-12149
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.93.22.12142
PMC: PMC37957
OpenAlex: W1983345237
Cited by: 859
References: 77
Citations by year: 2026: 10 · 2025: 8 · 2024: 11 · 2023: 19 · 2022: 8 · 2021: 6 · 2020: 16 · 2019: 11 · 2018: 19 · 2017: 19 · 2016: 21 · 2015: 28 · 2014: 25 · 2013: 21 · 2012: 30
FWCI: 9.34
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: N-end rule, protein half-life, N-terminal residues, ubiquitin system, protein degradation, ubiquitination, protein stability
MeSH terms: Acyltransferases, Amidohydrolases, Amino Acid Sequence, Animals, Female, Fungal Proteins, Half-Life, Ligases, Male, Models, Biological, Models, Chemical, Protein Conformation, Proteins, Rabbits, Proto-Oncogene Proteins c-mos, Evolution, Molecular, GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, Mice

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