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Journal articles on the topic 'The N-end rule'

Author: Grafiati

Published: 7 July 2024

Last updated: 31 July 2025

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1

Varshavsky, A. "The N-end Rule." Cold Spring Harbor Symposia on Quantitative Biology 60 (January 1, 1995): 461–78. http://dx.doi.org/10.1101/sqb.1995.060.01.051.

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2

Varshavsky, Alexander. "The N-end rule." Cell 69, no. 5 (1992): 725–35. http://dx.doi.org/10.1016/0092-8674(92)90285-k.

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3

Tasaki, Takafumi, Shashikanth M. Sriram, Kyong Soo Park, and Yong Tae Kwon. "The N-End Rule Pathway." Annual Review of Biochemistry 81, no. 1 (2012): 261–89. http://dx.doi.org/10.1146/annurev-biochem-051710-093308.

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4

Tobias, J., T. Shrader, G. Rocap, and A. Varshavsky. "The N-end rule in bacteria." Science 254, no. 5036 (1991): 1374–77. http://dx.doi.org/10.1126/science.1962196.

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5

Hurtley, Stella M. "Another N-end rule to add." Science 362, no. 6418 (2018): 1014.11–1016. http://dx.doi.org/10.1126/science.362.6418.1014-k.

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6

Kim, Jeong-Mok, and Cheol-Sang Hwang. "Crosstalk between the Arg/N-end and Ac/N-end rule." Cell Cycle 13, no. 9 (2014): 1366–67. http://dx.doi.org/10.4161/cc.28751.

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7

Eldeeb, Mohamed, and Richard Fahlman. "The-N-End Rule: The Beginning Determines the End." Protein & Peptide Letters 23, no. 4 (2016): 343–48. http://dx.doi.org/10.2174/0929866523666160108115809.

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8

Varshavsky, Alexander. "The N-end rule at atomic resolution." Nature Structural & Molecular Biology 15, no. 12 (2008): 1238–40. http://dx.doi.org/10.1038/nsmb1208-1238.

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9

Wojcik, Cezary. "Dipeptides: rulers of the N-end rule." Trends in Cell Biology 10, no. 9 (2000): 367. http://dx.doi.org/10.1016/s0962-8924(00)01827-4.

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10

Dougan, David A., and Alexander Varshavsky. "Understanding the Pro/N-end rule pathway." Nature Chemical Biology 14, no. 5 (2018): 415–16. http://dx.doi.org/10.1038/s41589-018-0045-0.

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11

Varshavsky, A. "The N-end rule: functions, mysteries, uses." Proceedings of the National Academy of Sciences 93, no. 22 (1996): 12142–49. http://dx.doi.org/10.1073/pnas.93.22.12142.

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12

Davydov, Ilia V., Debabrata Patra, and Alexander Varshavsky. "The N-End Rule Pathway inXenopusEgg Extracts." Archives of Biochemistry and Biophysics 357, no. 2 (1998): 317–25. http://dx.doi.org/10.1006/abbi.1998.0829.

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13

Eldeeb, Mohamed A., Luana C. A. Leitao, and Richard P. Fahlman. "Emerging branches of the N-end rule pathways are revealing the sequence complexities of N-termini dependent protein degradation." Biochemistry and Cell Biology 96, no. 3 (2018): 289–94. http://dx.doi.org/10.1139/bcb-2017-0274.

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The N-end rule links the identity of the N-terminal amino acid of a protein to its in vivo half-life, as some N-terminal residues confer metabolic instability to a protein via their recognition by the cellular machinery that targets them for degradation. Since its discovery, the N-end rule has generally been defined as set of rules of whether an N-terminal residue is stabilizing or not. However, recent studies are revealing that the N-terminal code of amino acids conferring protein instability is more complex than previously appreciated, as recent investigations are revealing that the identity

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14

Madura, K., R. J. Dohmen, and A. Varshavsky. "N-recognin/Ubc2 interactions in the N-end rule pathway." Journal of Biological Chemistry 268, no. 16 (1993): 12046–54. http://dx.doi.org/10.1016/s0021-9258(19)50306-4.

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15

Sriram, Shashikanth M., and Yong Tae Kwon. "The molecular principles of N-end rule recognition." Nature Structural & Molecular Biology 17, no. 10 (2010): 1164–65. http://dx.doi.org/10.1038/nsmb1010-1164.

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16

Varshavsky, Alexander. "The N-end rule and regulation of apoptosis." Nature Cell Biology 5, no. 5 (2003): 373–76. http://dx.doi.org/10.1038/ncb0503-373.

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17

Kwon, Yong Tae, Frédéric Lévy, and Alexander Varshavsky. "Bivalent Inhibitor of the N-end Rule Pathway." Journal of Biological Chemistry 274, no. 25 (1999): 18135–39. http://dx.doi.org/10.1074/jbc.274.25.18135.

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18

Varshavsky, Alexander. "The N-end rule pathway of protein degradation." Genes to Cells 2, no. 1 (1997): 13–28. http://dx.doi.org/10.1046/j.1365-2443.1997.1020301.x.

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19

Hurtley, Stella M. "The N-end rule finds a physiological function." Science Signaling 8, no. 368 (2015): ec65-ec65. http://dx.doi.org/10.1126/scisignal.aab1180.

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20

Gonda, D. K., A. Bachmair, I. Wünning, J. W. Tobias, W. S. Lane, and A. Varshavsky. "Universality and Structure of the N-end Rule." Journal of Biological Chemistry 264, no. 28 (1989): 16700–16712. http://dx.doi.org/10.1016/s0021-9258(19)84762-2.

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21

Wang, Kevin H., Giselle Roman-Hernandez, Robert A. Grant, Robert T. Sauer, and Tania A. Baker. "The Molecular Basis of N-End Rule Recognition." Molecular Cell 32, no. 3 (2008): 406–14. http://dx.doi.org/10.1016/j.molcel.2008.08.032.

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22

Hurtley, S. M. "The N-end rule finds a physiological function." Science 347, no. 6227 (2015): 1213. http://dx.doi.org/10.1126/science.347.6227.1213-q.

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23

Kim, Sung Tae, Takafumi Tasaki, Adriana Zakrzewska, et al. "The N-end rule proteolytic system in autophagy." Autophagy 9, no. 7 (2013): 1100–1103. http://dx.doi.org/10.4161/auto.24643.

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24

VARSHAVSKY, A. "The N-end rule pathway: Functions and mechanisms." Cell Biology International Reports 14 (September 1990): 8. http://dx.doi.org/10.1016/0309-1651(90)90142-l.

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25

Merkel, Lars, Henning S. G. Beckmann, Valentin Wittmann, and Nediljko Budisa. "Efficient N-Terminal Glycoconjugation of Proteins by the N-End Rule." ChemBioChem 9, no. 8 (2008): 1220–24. http://dx.doi.org/10.1002/cbic.200800050.

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26

Graciet, Emmanuelle, and Frank Wellmer. "The plant N-end rule pathway: structure and functions." Trends in Plant Science 15, no. 8 (2010): 447–53. http://dx.doi.org/10.1016/j.tplants.2010.04.011.

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27

Dougan, D. A., K. N. Truscott, and K. Zeth. "The bacterial N-end rule pathway: expect the unexpected." Molecular Microbiology 76, no. 3 (2010): 545–58. http://dx.doi.org/10.1111/j.1365-2958.2010.07120.x.

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28

Yamano, Koji, and Richard J. Youle. "PINK1 is degraded through the N-end rule pathway." Autophagy 9, no. 11 (2013): 1758–69. http://dx.doi.org/10.4161/auto.24633.

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29

Varshavsky, Alexander. "The N-end rule pathway and regulation by proteolysis." Protein Science 20, no. 8 (2011): 1298–345. http://dx.doi.org/10.1002/pro.666.

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30

Bartel, B., I. Wünning, and A. Varshavsky. "The recognition component of the N-end rule pathway." EMBO Journal 9, no. 10 (1990): 3179–89. http://dx.doi.org/10.1002/j.1460-2075.1990.tb07516.x.

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31

Oh, Jang-Hyun, Ju-Yeon Hyun, and Alexander Varshavsky. "Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway." Proceedings of the National Academy of Sciences 114, no. 22 (2017): E4370—E4379. http://dx.doi.org/10.1073/pnas.1705898114.

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We found that the heat shock protein 90 (Hsp90) chaperone system of the yeast Saccharomyces cerevisiae is greatly impaired in naa10Δ cells, which lack the NatA Nα-terminal acetylase (Nt-acetylase) and therefore cannot N-terminally acetylate a majority of normally N-terminally acetylated proteins, including Hsp90 and most of its cochaperones. Chk1, a mitotic checkpoint kinase and a client of Hsp90, was degraded relatively slowly in wild-type cells but was rapidly destroyed in naa10Δ cells by the Arg/N-end rule pathway, which recognized a C terminus-proximal degron of Chk1. Diverse proteins (in

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32

Siepmann, Thomas J., Richard N. Bohnsack, Zeynep Tokgöz, Olga V. Baboshina, and Arthur L. Haas. "Protein Interactions within the N-end Rule Ubiquitin Ligation Pathway." Journal of Biological Chemistry 278, no. 11 (2003): 9448–57. http://dx.doi.org/10.1074/jbc.m211240200.

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33

Baker, R. T., and A. Varshavsky. "Inhibition of the N-end rule pathway in living cells." Proceedings of the National Academy of Sciences 88, no. 4 (1991): 1090–94. http://dx.doi.org/10.1073/pnas.88.4.1090.

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34

Madura, K., and A. Varshavsky. "Degradation of G alpha by the N-end rule pathway." Science 265, no. 5177 (1994): 1454–58. http://dx.doi.org/10.1126/science.8073290.

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35

Hu, R. G., H. Wang, Z. Xia, and A. Varshavsky. "The N-end rule pathway is a sensor of heme." Proceedings of the National Academy of Sciences 105, no. 1 (2007): 76–81. http://dx.doi.org/10.1073/pnas.0710568105.

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36

Tasaki, Takafumi, Adriana Zakrzewska, Drew D. Dudgeon, Yonghua Jiang, John S. Lazo, and Yong Tae Kwon. "The Substrate Recognition Domains of the N-end Rule Pathway." Journal of Biological Chemistry 284, no. 3 (2008): 1884–95. http://dx.doi.org/10.1074/jbc.m803641200.

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37

Kim, Jeong-Mok, Ok-Hee Seok, Shinyeong Ju, et al. "Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway." Science 362, no. 6418 (2018): eaat0174. http://dx.doi.org/10.1126/science.aat0174.

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In bacteria, nascent proteins bear the pretranslationally generated N-terminal (Nt) formyl-methionine (fMet) residue. Nt-fMet of bacterial proteins is a degradation signal, termed fMet/N-degron. By contrast, proteins synthesized by cytosolic ribosomes of eukaryotes were presumed to bear unformylated Nt-Met. Here we found that the yeast formyltransferase Fmt1, although imported into mitochondria, could also produce Nt-formylated proteins in the cytosol. Nt-formylated proteins were strongly up-regulated in stationary phase or upon starvation for specific amino acids. This up-regulation strictly

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38

Wang, Haiqing, Konstantin I. Piatkov, Christopher S. Brower, and Alexander Varshavsky. "Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway." Molecular Cell 34, no. 6 (2009): 686–95. http://dx.doi.org/10.1016/j.molcel.2009.04.032.

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39

Wadas, Brandon, Jimo Borjigin, Zheping Huang, Jang-Hyun Oh, Cheol-Sang Hwang, and Alexander Varshavsky. "Degradation of SerotoninN-Acetyltransferase, a Circadian Regulator, by the N-end Rule Pathway." Journal of Biological Chemistry 291, no. 33 (2016): 17178–96. http://dx.doi.org/10.1074/jbc.m116.734640.

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SerotoninN-acetyltransferase (AANAT) converts serotonin toN-acetylserotonin (NAS), a distinct biological regulator and the immediate precursor of melatonin, a circulating hormone that influences circadian processes, including sleep. N-terminal sequences of AANAT enzymes vary among vertebrates. Mechanisms that regulate the levels of AANAT are incompletely understood. Previous findings were consistent with the possibility that AANAT may be controlled through its degradation by the N-end rule pathway. By expressing the rat and human AANATs and their mutants not only in mammalian cells but also in

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40

Kwon, Yong Tae, Zanxian Xia, Ilia V. Davydov, Stewart H. Lecker та Alexander Varshavsky. "Construction and Analysis of Mouse Strains Lacking the Ubiquitin Ligase UBR1 (E3α) of the N-End Rule Pathway". Molecular and Cellular Biology 21, № 23 (2001): 8007–21. http://dx.doi.org/10.1128/mcb.21.23.8007-8021.2001.

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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. In the yeast Saccharomyces cerevisiae, the UBR1-encoded ubiquitin ligase (E3) of the N-end rule pathway mediates the targeting of substrate proteins in part through binding to their destabilizing N-terminal residues. The functions of the yeast N-end rule pathway include fidelity of chromosome segregation and the regulation of peptide import. Our previous work described the cloning of cDNA and a gene encoding the 200-kDa mouse UBR1 (E3α). Here we show that mouse UBR1, in the presence of

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41

Eldeeb, Mohamed, Richard Fahlman, Mansoore Esmaili, and Mohamed Ragheb. "Regulating Apoptosis by Degradation: The N-End Rule-Mediated Regulation of Apoptotic Proteolytic Fragments in Mammalian Cells." International Journal of Molecular Sciences 19, no. 11 (2018): 3414. http://dx.doi.org/10.3390/ijms19113414.

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A pivotal hallmark of some cancer cells is the evasion of apoptotic cell death. Importantly, the initiation of apoptosis often results in the activation of caspases, which, in turn, culminates in the generation of proteolytically-activated protein fragments with potentially new or altered roles. Recent investigations have revealed that the activity of a significant number of the protease-generated, activated, pro-apoptotic protein fragments can be curbed via their selective degradation by the N-end rule degradation pathways. Of note, previous work revealed that several proteolytically-generate

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42

Lin, Chih-Cheng, Ya-Ting Chao, Wan-Chieh Chen, et al. "Regulatory cascade involving transcriptional and N-end rule pathways in rice under submergence." Proceedings of the National Academy of Sciences 116, no. 8 (2019): 3300–3309. http://dx.doi.org/10.1073/pnas.1818507116.

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The rice SUB1A-1 gene, which encodes a group VII ethylene response factor (ERFVII), plays a pivotal role in rice survival under flooding stress, as well as other abiotic stresses. In Arabidopsis, five ERFVII factors play roles in regulating hypoxic responses. A characteristic feature of Arabidopsis ERFVIIs is a destabilizing N terminus, which functions as an N-degron that targets them for degradation via the oxygen-dependent N-end rule pathway of proteolysis, but permits their stabilization during hypoxia for hypoxia-responsive signaling. Despite having the canonical N-degron sequence, SUB1A-1

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43

Mulder, Lubbertus C. F., and Mark A. Muesing. "Degradation of HIV-1 Integrase by the N-end Rule Pathway." Journal of Biological Chemistry 275, no. 38 (2000): 29749–53. http://dx.doi.org/10.1074/jbc.m004670200.

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44

Graciet, Emmanuelle, Francesca Mesiti, and Frank Wellmer. "Structure and evolutionary conservation of the plant N-end rule pathway." Plant Journal 61, no. 5 (2010): 741–51. http://dx.doi.org/10.1111/j.1365-313x.2009.04099.x.

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45

Gibbs, Daniel J., Jaume Bacardit, Andreas Bachmair, and Michael J. Holdsworth. "The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions." Trends in Cell Biology 24, no. 10 (2014): 603–11. http://dx.doi.org/10.1016/j.tcb.2014.05.001.

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46

Liu, Yujiao, Chao Liu, Wen Dong, and Wei Li. "Physiological functions and clinical implications of the N-end rule pathway." Frontiers of Medicine 10, no. 3 (2016): 258–70. http://dx.doi.org/10.1007/s11684-016-0458-7.

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47

Boso, Guney, Takafumi Tasaki, Yong Kwon, and Nikunj V. Somia. "The N-end rule and retroviral infection: no effect on integrase." Virology Journal 10, no. 1 (2013): 233. http://dx.doi.org/10.1186/1743-422x-10-233.

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48

Wang, Kevin H., Elizabeth S. C. Oakes, Robert T. Sauer, and Tania A. Baker. "Tuning the Strength of a Bacterial N-end Rule Degradation Signal." Journal of Biological Chemistry 283, no. 36 (2008): 24600–24607. http://dx.doi.org/10.1074/jbc.m802213200.

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49

Nguyen, Kha The, Sang-Hyeon Mun, Chang-Seok Lee, and Cheol-Sang Hwang. "Control of protein degradation by N-terminal acetylation and the N-end rule pathway." Experimental & Molecular Medicine 50, no. 7 (2018): 1–8. http://dx.doi.org/10.1038/s12276-018-0097-y.

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50

Chui, Ashley J., Marian C. Okondo, Sahana D. Rao, et al. "N-terminal degradation activates the NLRP1B inflammasome." Science 364, no. 6435 (2019): 82–85. http://dx.doi.org/10.1126/science.aau1208.

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Intracellular pathogens and danger signals trigger the formation of inflammasomes, which activate inflammatory caspases and induce pyroptosis. The anthrax lethal factor metalloprotease and small-molecule DPP8/9 inhibitors both activate the NLRP1B inflammasome, but the molecular mechanism of NLRP1B activation is unknown. In this study, we used genome-wide CRISPR-Cas9 knockout screens to identify genes required for NLRP1B-mediated pyroptosis. We discovered that lethal factor induces cell death via the N-end rule proteasomal degradation pathway. Lethal factor directly cleaves NLRP1B, inducing the

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