Them subunit of murine translation initiation factor eIF3 maintains the integrity of the eIF3 complex and is required for embryonic development, homeostasis, and organ size control

Journal of Biological Chemistry

Volumn 288, Issue 42, 2013, Pages 30087-30093

  Zeng, Liyong ^a   Wan, Yihan ^a   Li, Dan ^a   Wu, Jing ^c   Shao, Mengle ^b   Chen, Jiong ^c   Hui, Lijian ^a   Ji, Hongbin ^a   Zhu, Xueliang ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b Shanghai Jiao Tong University Affiliated Sixth People s Hospital   (China)

^c NANJING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

COMPLEX FORMATIONS; EMBRYONIC DEVELOPMENT; EUKARYOTIC TRANSLATION; INITIATION FACTORS; PHYSIOLOGICAL FUNCTIONS; SIZE CONTROL;

PHYSIOLOGY;

CRE RECOMBINASE; FATTY ACID BINDING PROTEIN 4; INITIATION FACTOR 3; INITIATION FACTOR 3F; INITIATION FACTOR 3H; INITIATION FACTOR 3M; UNCLASSIFIED DRUG; MULTIPROTEIN COMPLEX;

ADULT ANIMAL; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BIOGENESIS; BODY WEIGHT; CONTROLLED STUDY; DEATH; DOWN REGULATION; EIF3M GENE; EMBRYO; EMBRYO DEVELOPMENT; FEMALE; GESTATION PERIOD; HAPLOINSUFFICIENCY; HETEROZYGOTE; HOMEOSTASIS; HUMAN; HUMAN CELL; LETHALITY; LIVER WEIGHT; MOUSE; NONHUMAN; ORGAN SIZE; PREIMPLANTATION EMBRYO; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEPLETION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; WEIGHT REDUCTION; ANIMAL; BIOSYNTHESIS; GENE EXPRESSION REGULATION; GENETICS; HEK293 CELL LINE; KNOCKOUT MOUSE; LIVER; METABOLISM; NIDATION; PHYSIOLOGY; PROTEIN SYNTHESIS; CELL STRAIN HEK293; EUKARYOTIC INITIATION FACTOR; KNOCK-OUT MICE; MOUSE GENETICS; PROTEIN COMPLEXES; TRANSLATION INITIATION FACTORS;

ANIMALIA; EUKARYOTA; MURINAE; MUS;

ANIMALS; EMBRYO IMPLANTATION; EUKARYOTIC INITIATION FACTOR-3; GENE EXPRESSION REGULATION, DEVELOPMENTAL; HEK293 CELLS; HETEROZYGOTE; HOMEOSTASIS; HUMANS; LIVER; MICE; MICE, KNOCKOUT; MULTIPROTEIN COMPLEXES; ORGAN SIZE; PROTEIN BIOSYNTHESIS;

EMBRYO; EUKARYOTIC INITIATION FACTOR; KNOCK-OUT MICE; MOUSE GENETICS; PROTEIN COMPLEXES; PROTEIN STABILITY; TRANSLATION INITIATION FACTORS;

EID: 84886941531     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.506147     Document Type: Article

References (36)

1. Jackson, R. J., Hellen, C. U., and Pestova, T. V. (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 11, 113-127
2. Aitken, C. E., and Lorsch, J. R. (2012) A mechanistic overview of translation initiation in eukaryotes. Nat. Struct. Mol. Biol. 19, 568-576
3. Hinnebusch, A. G., and Lorsch, J. R. (2012) The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol. 4, a011544
4. Zoncu, R., Efeyan, A., and Sabatini, D. M. (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35
5. Santini, E., Huynh, T. N., MacAskill, A. F., Carter, A. G., Pierre, P., Ruggero, D., Kaphzan, H., and Klann, E. (2013) Exaggerated translation causes synaptic and behavioural aberrations associated with autism. Nature 493, 411-415
6. Silvera, D., Formenti, S. C., and Schneider, R. J. (2010) Translational control in cancer. Nat. Rev. Cancer 10, 254-266
7. Rogers, A. N., Chen, D., McColl, G., Czerwieniec, G., Felkey, K., Gibson, B. W., Hubbard, A., Melov, S., Lithgow, G. J., and Kapahi, P. (2011) Life span extension via eIF4G inhibition is mediated by posttranscriptional remodeling of stress response gene expression in C. elegans. Cell Metab 14, 55-66
8. Curran, S. P., and Ruvkun, G. (2007) Lifespan regulation by evolutionarily conserved genes essential for viability. PLoS Genet. 3, e56
9. Pick, E., Hofmann, K., and Glickman, M. H. (2009) PCI complexes: beyond the proteasome, CSN, and eIF3 Troika. Mol. Cell 35, 260-264
10. Chaudhuri, J., Chowdhury, D., and Maitra, U. (1999) Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex. J. Biol. Chem. 274, 17975-17980
11. Holz, M. K., Ballif, B. A., Gygi, S. P., and Blenis, J. (2005) mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569-580
12. Sha, Z., Brill, L. M., Cabrera, R., Kleifeld, O., Scheliga, J. S., Glickman, M. H., Chang, E. C., and Wolf, D. A. (2009) The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries. Mol. Cell 36, 141-152
13. Siridechadilok, B., Fraser, C. S., Hall, R. J., Doudna, J. A., and Nogales, E. (2005) Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310, 1513-1515
14. Masutani, M., Sonenberg, N., Yokoyama, S., and Imataka, H. (2007) Reconstitution reveals the functional core of mammalian eIF3. EMBO J. 26, 3373-3383
15. Fraser, C. S., Lee, J. Y., Mayeur, G. L., Bushell, M., Doudna, J. A., and Hershey, J. W. (2004) The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro. J. Biol. Chem. 279, 8946-8956
16. Zhou, M., Sandercock, A. M., Fraser, C. S., Ridlova, G., Stephens, E., Schenauer, M. R., Yokoi-Fong, T., Barsky, D., Leary, J. A., Hershey, J. W., Doudna, J. A., and Robinson, C. V. (2008) Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. Proc. Natl. Acad. Sci. U.S.A. 105, 18139-18144
17. Goh, S. H., Hong, S. H., Hong, S. H., Lee, B. C., Ju, M. H., Jeong, J. S., Cho, Y. R., Kim, I. H., and Lee, Y. S. (2011) eIF3m expression influences the regulation of tumorigenesis-related genes in human colon cancer. Oncogene 30, 398-409
18. Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H. P., Greenberg, J. R., Qin, J., and Hinnebusch, A. G. (1998) Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol. 18, 4935-4946
19. Zhou, C., Arslan, F., Wee, S., Krishnan, S., Ivanov, A. R., Oliva, A., Leatherwood, J., and Wolf, D. A. (2005) PCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes. BMC Biol. 3, 14
20. Akagi, K., Sandig, V., Vooijs, M., Van der Valk, M., Giovannini, M., Strauss, M., and Berns, A. (1997) Cre-mediated somatic site-specific recombination in mice. Nucleic Acids Res. 25, 1766-1773
21. Min, L., Ji, Y., Bakiri, L., Qiu, Z., Cen, J., Chen, X., Chen, L., Scheuch, H., Zheng, H., Qin, L., Zatloukal, K., Hui, L., and Wagner, E. F. (2012) Liver cancer initiation is controlled by AP-1 through SIRT6-dependent inhibition of survivin. Nat. Cell Biol. 14, 1203-1211
22. Xu, J. (2005) Preparation, culture, and immortalization of mouse embryonic fibroblasts. Curr. Protoc. Mol. Biol. Chapter 28, Unit 28.21, 10.1002/0471142727.mb2801s70
23. Wang, F., Zhang, Q., Cao, J., Huang, Q., and Zhu, X. (2008) The microtubule plus end-binding protein EB1 is involved in Sertoli cell plasticity in testicular seminiferous tubules. Exp. Cell Res. 314, 213-226
24. Lois, C., Hong, E. J., Pease, S., Brown, E. J., and Baltimore, D. (2002) Germline transmission and tissue-specific expression of transgenes delivered by lentiviral vectors. Science 295, 868-872
25. He, T. C., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., and Vogelstein, B. (1998) A simplified system for generating recombinant adenoviruses. Proc. Natl. Acad. Sci. U.S.A. 95, 2509-2514
26. Zhou, Q., Chen, D., Pierstorff, E., and Luo, K. (1998) Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages. EMBO J. 17, 3681-3691
27. Lakso, M., Pichel, J. G., Gorman, J. R., Sauer, B., Okamoto, Y., Lee, E., Alt, F. W., and Westphal, H. (1996) Efficient in vivo manipulation of mouse genomic sequences at the zygote stage. Proc. Natl. Acad. Sci. U.S.A. 93, 5860-5865
28. Hirotsune, S., Fleck, M. W., Gambello, M. J., Bix, G. J., Chen, A., Clark, G. D., Ledbetter, D. H., McBain, C. J., and Wynshaw-Boris, A. (1998) Graded reduction of Pafah1b1 (Lis1) activity results in neuronal migration defects and early embryonic lethality. Nat. Genet. 19, 333-339
29. He, W., Barak, Y., Hevener, A., Olson, P., Liao, D., Le, J., Nelson, M., Ong, E., Olefsky, J. M., and Evans, R. M. (2003) Adipose-specific peroxisome proliferator-activated receptor knockout causes insulin resistance in fat and liver but not in muscle. Proc. Natl. Acad. Sci. U.S.A. 100, 15712-15717
30. Derivery, E., and Gautreau, A. (2010) Generation of branched actin networks: assembly and regulation of the N-WASP and WAVE molecular machines. BioEssays 32, 119-131
31. Wickner, S., Maurizi, M. R., and Gottesman, S. (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286, 1888-1893
32. Wu, S., Ma, L., Wu, Y., Zeng, R., and Zhu, X. (2012) Nudel is crucial for the WAVE complex assembly in vivo by selectively promoting subcomplex stability and formation through direct interactions. Cell Res. 22, 1270-1284
33. Sasaki, S., Mori, D., Toyo-oka, K., Chen, A., Garrett-Beal, L., Muramatsu, M., Miyagawa, S., Hiraiwa, N., Yoshiki, A., Wynshaw-Boris, A., and Hirotsune, S. (2005) Complete loss of Ndel1 results in neuronal migration defects and early embryonic lethality. Mol. Cell. Biol. 25, 7812-7827
34. Satterfield, M. C., and Wu, G. (2011) Brown adipose tissue growth and development: significance and nutritional regulation. Front. Biosci. 16, 1589-1608
35. Urs, S., Harrington, A., Liaw, L., and Small, D. (2006) Selective expression of an aP2/fatty acid binding protein 4-Cre transgene in non-adipogenic tissues during embryonic development. Transgenic Res. 15, 647-653
36. Billon, N., Monteiro, M. C., and Dani, C. (2008) Developmental origin of adipocytes: new insights into a pending question. Biol. Cell 100, 563-575