Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway

Molecular Cell

Volumn 34, Issue 6, 2009, Pages 686-695

  Wang, Haiqing ^a   Piatkov, Konstantin I ^a   Brower, Christopher S ^a   Varshavsky, Alexander ^a  

^a CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

PROTEINS

Indexed keywords

AMIDASE; GLUTAMINE; MUTANT PROTEIN; N TERMINAL AMIDASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN ANALYSIS; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; CLONING, MOLECULAR; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GLUTAMINE; HALF-LIFE; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NIH 3T3 CELLS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

ANIMALIA; BOVINAE; FUNGI;

EID: 67449146916     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.04.032     Document Type: Article

References (37)

1. An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., and Kwon Y.T. Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. Proc. Natl. Acad. Sci. USA 103 (2006) 6212-6217
2. Bachmair A., and Varshavsky A. The degradation signal in a short-lived protein. Cell 56 (1989) 1019-1032
3. Baker R.T., and Varshavsky A. Yeast N-terminal amidase: a new enzyme and component of the N-end rule pathway. J. Biol. Chem. 270 (1995) 12065-12074
4. Dubnau J., Chiang A.-S., Grady L., Barditch J., Gossweiler S., McNeil J., Smith P., Buldoc F., Scott R., Certa U., et al. The staufen/pumilio pathway is involved in Drosophila long-term memory. Curr. Biol. 13 (2003) 286-296
5. Dutton A., and Singer S.J. Crosslinking and labeling of membrane proteins by transglutaminase-catalyzed reactions. Proc. Natl. Acad. Sci. USA 72 (1975) 2568-2571
6. Eisele F., and Wolf D.H. Degradation of misfolded proteins in the cytoplasm by the ubiquitin ligase Ubr1. FEBS Lett. 582 (2008) 4143-4146
7. Graciet E., Hu R.G., Piatkov K., Rhee J.H., Schwarz E.M., and Varshavsky A. Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen. Proc. Natl. Acad. Sci. USA 103 (2006) 3078-3083
8. Grigoryev S., Stewart A.E., Kwon Y.T., Arfin S.M., Bradshaw R.A., Jenkins N.A., Copeland N.G., and Varshavsky A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271 (1996) 28521-28532
9. Holman T.J., Jones P.D., Russell L., Medhurst A., Ubeda T.S., Talloji P., Marquez J., Schmuths H., Tung S.A., Taylor I., et al. The N-end rule pathway promotes seed germination and establishment through removal of ABA sensitivity in Arabidopsis. Proc. Natl. Acad. Sci. USA 106 (2009) 4549-4554
10. Hu R.-G., Sheng J., Xin Q., Xu Z., Takahashi T.T., and Varshavsky A. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Nature 437 (2005) 981-986
11. Hu R.-G., Wang H., Xia Z., and Varshavsky A. The N-end rule pathway is a sensor of heme. Proc. Natl. Acad. Sci. USA 105 (2008) 76-81
12. Huang T.T., Nijman S.M.B., Mirchandani K.D., Galardy P.J., Cohn M.A., Haas W., Gygi S.P., Ploegh H.P., Bernards R., and D'Andrea A.D. Regulation of monoubiquitinated PCNA by DUB autocleavage. Nat. Cell Biol. 8 (2006) 339-347
13. Hwang C.-S., and Varshavsky A. Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway. Proc. Natl. Acad. Sci. USA 105 (2008) 19188-19193
14. Hwang C.-S., Shemorry A., and Varshavsky A. Two proteolytic pathways regulate DNA repair by co-targeting the Mgt1 alkyguanine transferase. Proc. Natl. Acad. Sci. USA 106 (2009) 2142-2147
15. Johnson E.S., Gonda D.K., and Varshavsky A. Cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature 346 (1990) 287-291
16. Kwon Y.T., Balogh S.A., Davydov I.V., Kashina A.S., Yoon J.K., Xie Y., Gaur A., Hyde L., Denenberg V.H., and Varshavsky A. Altered activity, social behavior, and spatial memory in mice lacking the NTAN1 amidase and the asparagine branch of the N-end rule pathway. Mol. Cell. Biol. 20 (2000) 4135-4148
17. Kwon Y.T., Kashina A.S., Davydov I.V., Hu R.-G., An J.Y., Seo J.W., Du F., and Varshavsky A. An essential role of N-terminal arginylation in cardiovascular development. Science 297 (2002) 96-99
18. Lim J., Hao T., Shaw C., Patel A.J., Szabó G., Rual J.-F., Fisk C.J., Li N., Smolyar A., Hill D.E., et al. A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. Cell 125 (2006) 801-814
19. Mogk A., Schmidt R., and Bukau B. The N-end rule pathway of regulated proteolysis: prokaryotic and eukaryotic strategies. Trends Cell Biol. 17 (2007) 165-172
20. Pedersen L.C., Yee V.C., Bishop P.D., Le Trong I., Teller D.C., and Stenkamp R.E. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Protein Sci. 3 (1994) 1131-1135
21. Prakash S., Inobe T., Hatch A.J., and Matouschek A. Substrate selection by the proteasome during degradation of protein complexes. Nat. Chem. Biol. 5 (2009) 29-36
22. Rao H., Uhlmann F., Nasmyth K., and Varshavsky A. Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature 410 (2001) 955-960
23. Ravid T., and Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat. Rev. Mol. Cell Biol. 9 (2008) 679-689
24. Schilling S., Wasternack C., and Demuth H.U. Glutaminyl cyclases from animal and plants: a case of functionally convergent evolution. Biol. Chem. 389 (2008) 983-991
25. Suzuki T., and Varshavsky A. Degradation signals in the lysine-asparagine sequence space. EMBO J. 18 (1999) 6017-6026
26. Tasaki T., and Kwon Y.T. The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci. 32 (2007) 520-528
27. Tasaki T., Zakrzewska A., Dudgeon D., Jiang Y., Lazo J.S., and Kwon Y.T. The substrate recognition domains of the N-end rule pathway. J. Biol. Chem. 284 (2009) 1884-1895
28. Tian L., Wang P., Guo J., Wang X., Deng W., Zhang C., Fu D., Gao X., Shi T., and Ma D. Screening for novel human genes associated with CRE pathway activation with cell microarray. Genomics 90 (2007) 28-34
29. Varshavsky A. The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 93 (1996) 12142-12149
30. Varshavsky A. Spalog and sequelog: neutral terms for spatial and sequence similarity. Curr. Biol. 14 (2004) R181-R183
31. Varshavsky A. Ubiquitin fusion technique and related methods. Methods Enzymol. 399 (2005) 777-799
32. Varshavsky A. Discovery of cellular regulation by protein degradation. J. Biol. Chem. 283 (2008) 34469-34489
33. Varshavsky A. The N-end rule at atomic resolution. Nat. Struct. Mol. Biol. 15 (2008) 1238-1240
34. Wang K.H., Roman-Hernandez G., Grant R.A., Sauer T.T., and Baker T.A. The molecular basis of N-end rule recognition. Mol. Cell 32 (2008) 406-414
35. Xia Z., Turner G.C., Hwang C.-S., Byrd C., and Varshavsky A. Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter. J. Biol. Chem. 283 (2008) 28958-28968
36. Xia Z., Webster A., Du F., Piatkov K., Ghislain M., and Varshavsky A. Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway. J. Biol. Chem. 283 (2008) 24011-24028
37. Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K., Durie P.R., Beier M., Hülskamp G., Guzman C., Rehder H., et al. Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome). Nat. Genet. 37 (2005) 1345-1350