Erratum: Protection of Extraribosomal RPL13a by GAPDH and Dysregulation by S-Nitrosylation (Protection of Extraribosomal RPL13a by GAPDH and Dysregulation by S-Nitrosylation (2012) 47(4) (656–663), (S1097276512004996), (10.1016/j.molcel.2012.06.006));Protection of Extraribosomal RPL13a by GAPDH and Dysregulation by S-Nitrosylation

Molecular Cell

Volumn 47, Issue 4, 2012, Pages 656-663

  Jia, Jie ^a   Arif, Abul ^a   Willard, Belinda ^a   Smith, Jonathan D ^a   Stuehr, Dennis J ^a   Hazen, Stanley L ^a   Fox, Paul L ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CERULOPLASMIN; CHAPERONE; CYSTEINE; GAMMA INTERFERON; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; INTERFERON GAMMA ACTIVATED INHIBITO OF TRANSLATION COMPLEX; OXIDIZED LOW DENSITY LIPOPROTEIN; PROTEASOME; RIBOSOME PROTEIN; RIBOSOME PROTEIN L13A; UNCLASSIFIED DRUG; VASCULOTROPIN A;

ARTICLE; BONE MARROW CELL; CONTROLLED STUDY; HUMAN; HUMAN CELL; NITROSYLATION; PROTEIN DEGRADATION; PROTEIN PROCESSING;

EUKARYOTA;

EID: 84865361604     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2023.10.014     Document Type: Erratum

References (35)

1. Amsterdam A., Sadler K.C., Lai K., Farrington S., Bronson R.T., Lees J.A., Hopkins N. Many ribosomal protein genes are cancer genes in zebrafish. PLoS Biol. 2004, 2:E139.
2. Anderson P. Post-transcriptional regulons coordinate the initiation and resolution of inflammation. Nat. Rev. Immunol. 2010, 10:24-35.
3. Draptchinskaia N., Gustavsson P., Andersson B., Pettersson M., Willig T.N., Dianzani I., Ball S., Tchernia G., Klar J., Matsson H., et al. The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia. Nat. Genet. 1999, 21:169-175.
4. Flygare J., Karlsson S. Diamond-Blackfan anemia: erythropoiesis lost in translation. Blood 2007, 109:3152-3154.
5. Foster M.W., Hess D.T., Stamler J.S. Protein S-nitrosylation in health and disease: a current perspective. Trends Mol. Med. 2009, 15:391-404.
6. Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., et al. Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients. Am. J. Hum. Genet. 2008, 83:769-780.
7. Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y., Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat. Cell Biol. 2005, 7:665-674.
8. Jaffrey S.R., Erdjument-Bromage H., Ferris C.D., Tempst P., Snyder S.H. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat. Cell Biol. 2001, 3:193-197.
9. Jia J., Arif A., Ray P.S., Fox P.L. WHEP domains direct noncanonical function of glutamyl-Prolyl tRNA synthetase in translational control of gene expression. Mol. Cell 2008, 29:679-690.
10. Kankaanpää J., Turunen S.P., Moilanen V., Hörkkö S., Remes A.M. Cerebrospinal fluid antibodies to oxidized LDL are increased in Alzheimer's disease. Neurobiol. Dis. 2009, 33:467-472.
11. Kim T.S., Jang C.Y., Kim H.D., Lee J.Y., Ahn B.Y., Kim J. Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. Mol. Biol. Cell 2006, 17:824-833.
12. Libby P., Ridker P.M., Maseri A. Inflammation and atherosclerosis. Circulation 2002, 105:1135-1143.
13. Lindemann S.W., Weyrich A.S., Zimmerman G.A. Signaling to translational control pathways: diversity in gene regulation in inflammatory and vascular cells. Trends Cardiovasc. Med. 2005, 15:9-17.
14. Marino S.M., Gladyshev V.N. Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation. J. Mol. Biol. 2010, 395:844-859.
15. Mazumder B., Fox P.L. Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells: role of the 3' untranslated region. Mol. Cell. Biol. 1999, 19:6898-6905.
16. Mazumder B., Sampath P., Seshadri V., Maitra R.K., DiCorleto P.E., Fox P.L. Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control. Cell 2003, 115:187-198.
17. Medzhitov R., Horng T. Transcriptional control of the inflammatory response. Nat. Rev. Immunol. 2009, 9:692-703.
18. Mukhopadhyay R., Ray P.S., Arif A., Brady A.K., Kinter M., Fox P.L. DAPK-ZIPK-L13a axis constitutes a negative-feedback module regulating inflammatory gene expression. Mol. Cell 2008, 32:371-382.
19. Mukhopadhyay R., Jia J., Arif A., Ray P.S., Fox P.L. The GAIT system: a gatekeeper of inflammatory gene expression. Trends Biochem. Sci. 2009, 34:324-331.
20. Nakajima H., Amano W., Kubo T., Fukuhara A., Ihara H., Azuma Y.T., Tajima H., Inui T., Sawa A., Takeuchi T. Glyceraldehyde-3-phosphate dehydrogenase aggregate formation participates in oxidative stress-induced cell death. J. Biol. Chem. 2009, 284:34331-34341.
21. Nathan C. Points of control in inflammation. Nature 2002, 420:846-852.
22. Nomura M. Regulation of ribosome biosynthesis in Escherichia coli and Saccharomyces cerevisiae: diversity and common principles. J. Bacteriol. 1999, 181:6857-6864.
23. Podrez E.A., Febbraio M., Sheibani N., Schmitt D., Silverstein R.L., Hajjar D.P., Cohen P.A., Frazier W.A., Hoff H.F., Hazen S.L. Macrophage scavenger receptor CD36 is the major receptor for LDL modified by monocyte-generated reactive nitrogen species. J. Clin. Invest. 2000, 105:1095-1108.
24. Podrez E.A., Poliakov E., Shen Z., Zhang R., Deng Y., Sun M., Finton P.J., Shan L., Febbraio M., Hajjar D.P., et al. A novel family of atherogenic oxidized phospholipids promotes macrophage foam cell formation via the scavenger receptor CD36 and is enriched in atherosclerotic lesions. J. Biol. Chem. 2002, 277:38517-38523.
25. Ray P.S., Fox P.L. A post-transcriptional pathway represses monocyte VEGF-A expression and angiogenic activity. EMBO J. 2007, 26:3360-3372.
26. Ruvinsky I., Sharon N., Lerer T., Cohen H., Stolovich-Rain M., Nir T., Dor Y., Zisman P., Meyuhas O. Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis. Genes Dev. 2005, 19:2199-2211.
27. Sampath P., Mazumder B., Seshadri V., Fox P.L. Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3' untranslated region. Mol. Cell. Biol. 2003, 23:1509-1519.
28. Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L. Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Cell 2004, 119:195-208.
29. Shoji T., Fukumoto M., Kimoto E., Shinohara K., Emoto M., Tahara H., Koyama H., Ishimura E., Nakatani T., Miki T., et al. Antibody to oxidized low-density lipoprotein and cardiovascular mortality in end-stage renal disease. Kidney Int. 2002, 62:2230-2237.
30. Stocker R., Keaney J.F. Role of oxidative modifications in atherosclerosis. Physiol. Rev. 2004, 84:1381-1478.
31. Vyas K., Chaudhuri S., Leaman D.W., Komar A.A., Musiyenko A., Barik S., Mazumder B. Genome-wide polysome profiling reveals an inflammation-responsive posttranscriptional operon in gamma interferon-activated monocytes. Mol. Cell. Biol. 2009, 29:458-470.
32. Warner J.R. The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 1999, 24:437-440.
33. Warner J.R., McIntosh K.B. How common are extraribosomal functions of ribosomal proteins?. Mol. Cell 2009, 34:3-11.
34. Yao P., Potdar A.A., Arif A., Ray P.S., Mukhopadhyay R., Willard B., Xu Y., Yan J., Saidel G.M., Fox P.L. Coding region polyadenylation generates a truncated tRNA synthetase that counters translation repression. Cell 2012, 149:88-100.
35. Zheng L., Roeder R.G., Luo Y. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 2003, 114:255-266.