The translation initiation factor eIF2β is an interactor of protein phosphatase-1

Biochemical Journal

Volumn 400, Issue 2, 2006, Pages 377-383

  Wakula, Paulina ^a   Beullens, Monique ^a   Van Eynde, Aleyde ^a   Ceulemans, Hugo ^a   Stalmans, Willy ^a   Bollen, Mathieu ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

eIF2 ; Protein (de)phosphorylation; Protein phosphatase 1; Translation

Indexed keywords

BINDING ENERGY; BIOASSAY; CELLS; MUTAGENESIS; PHOSPHORUS COMPOUNDS; SUBSTRATES;

EUKARYOTIC TRANSLATION; IMMUNOPRECIPITATION ASSAYS; PROTEIN (DE)PHOSPHORYLATION; PROTEIN PHOSPHATASE-1;

ENZYME INHIBITION;

BACTERIAL PROTEIN; GLYCOGEN PHOSPHORYLASE; INITIATION FACTOR; INITIATION FACTOR 2ALPHA; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN ELF2BETA; SERINE;

ANIMAL CELL; ARTICLE; CELL LYSATE; CONTROLLED STUDY; DRUG INHIBITION; GENE MAPPING; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VIVO STUDY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEPHOSPHORYLATION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN PURIFICATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; EUKARYOTIC INITIATION FACTOR-2; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDE MAPPING; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN BIOSYNTHESIS; RABBITS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; SWINE;

EUKARYOTA;

EID: 33845226123     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060758     Document Type: Article

References (34)

1. Preiss, T. and Hentze, W. M. (2003) Starting the protein synthesis machine: eukaryotic translation initiation. Bioessays 25, 1201-1211
2. i release from eIF2, not GTP hydrolysis is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20, 251-262
3. Kimball, S. R. (1999) Eukaryotic initiation factor eIF2. Int. J. Biochem. Cell B. 31, 25-29
4. Holcik, M. and Sonenberg, N. (2005) Translational control in stress and apoptosis. Nat. Rev. Mol. Cell. Biol. 6, 318-327
5. Kapp, L. D. and Lorsch, J. R. (2004) The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 73, 657-704
6. Unbehaun, A., Borukhov, S. I., Hellen, C. U. and Pestova, T. V. (2004) Release of initiation factors from 48 S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev. 18, 3078-3093
7. Hashimoto, N. N., Carnevalli, L S. and Castilho, B. A. (2002) Translation initiation at non-AUG codons mediated by weakened association of eukaryotic initiation factor (eIF) 2 subunits. Biochem. J. 367, 359-368
8. Wang, X., Paulin, F. E., Campbell, L. E., Gomez, E., O'Brien, K., Morrice, N. and Proud, C. G. (2001) Eukaryotic initiation factor 2B: identification of multiple phosporylation sites in the epsilon-subunit and their functions in vivo. EMBO J. 20, 4349-4359
9. Paulin, F E., Campbell, L. E., O'Brien, K., Loughlin, J. and Proud, C. G. (2001) Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase activator protein. Curr. Biol. 11, 55-59
10. Das, S., Ghosh, R. and Maitra, U. (2001) Eukaryotic translation initiation factor 5 functions as a GTPase activating protein. J. Biol. Chem. 276, 6720-6726
11. Kimball, S. R., Heinzinger, N. K., Horetsky, R. L. and Jefferson, L. S. (1998) Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B. J. Biol. Chem. 273, 3039-3044
12. Ting, N. S., Kao, P. N., Chan, D. W., Lintott, L. G. and Lees-Miller, S. P. (1998) DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. J. Biol. Chem. 273, 2136-2145
13. Welsh, G., Price, N. T., Bladergroen, B. A., Bloomberg, G. and Proud, C. G. (1994) Identification of novel phosphorylation sites in the β-subunit of translation initiation factor eIF-2. Biochem. Biophys. Res. Commun. 201, 1279-1288
14. Ceulemans, H. and Bollen, M. (2004) Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol. Rev. 84, 1-39
15. Bollen, M. (2001) Combinatorial control of protein phosphatase-1. Trends Biochem. Sci. 26, 426-431
16. Wakula, P., Beullens, M., Ceulemans, H., Stalmans, W. and Bollen, M. (2003) Degeneracy and function of the ubiquitous RVXF motif that mediates binding to protein phosphatase-1. J. Biol. Chem. 278, 18817-18823
17. Egloff, M. P., Johnson, D. F., Moorhead, G., Cohen, P. T., Cohen, P. and Barford, D. (1997) Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16, 1876-1887
18. Ceulemans, H., Stalmans, W. and Bollen, M. (2002) Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution. Bioessays 24, 371-381
19. Meiselbach, H., Sticht, H. and Enz, R. (2006) Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins. Chem Biol. 13, 49-59
20. DeGuzman, A. and Lee, E. Y. C. (1988) Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase. Methods Enzymol. 159, 356-368
21. Fischer, E. H. and Krebs, E. G. (1958) The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J. Biol. Chem. 231, 65-71
22. Agostinis, P., Derua, R., Sarno, S., Goris, J. and Merlevede, W. (1992) Phosphorylation of the phosphatase modulator subunit (inhibitor-2) by casein kinase-1. FEBS Lett. 305, 121-124
23. Beullens, M., Van Eynde, A., Stalmans, W. and Bollen, M. (1992) The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei. J. Biol. Chem. 267, 16538-16544
24. Sander, C. and Schneider, R. (1991) Database of homology-derived structures and the structural meaning of sequence alignment. Proteins 9, 56-58
25. Bollen, M. and Stalmans, W. (1992) The structure, role, and regulation of type 1 protein phosphatases. Crit. Rev. Biochem. Mol. 27, 227-281
26. Beullens, M., Vancauwenbergh, S., Morrice, N., Derua, R., Ceulemans, H., Waelkens, E. and Bollen, M. (2005) Substrate specificity and activity regulation of protein kinase MELK. J. Biol. Chem. 280, 40003-40011
27. Jin, Q., Van Eynde, A., Beullens, M., Roy, N., Thiel, G., Stalmans, W. and Bollen, M. (2003) The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic development (EED), and functions as a transcriptional repressor. J. Biol. Chem. 278, 30677-30685
28. Beullens, M. and Bollen, M. (2002) The protein phosphatase-1 regulator NIPP1 is also a splicing factor involved in a late step of spliceosome assembly. J. Biol. Chem. 277, 19855-19860
29. Novoa, I., Zheng, H., Harding, H. P. and Ron, D. (2001) Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell Biol. 153, 1011-1022
30. Connor, J. H., Weiser, D. C., Li, S., Hallenbeck, J. M. and Shenolikar, S. (2001) Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol. Cell. Biol. 21, 6841-6850
31. Jousse, C., Oyadomari, S., Novoa, I., Lu, P., Zhang, Y., Harding, H. P. and Ron, D. (2003) Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CreP, promotes survival of stressed cells. J. Cell Biol. 163, 767-775
32. Bohnsack, M. T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E. and Gorlich, D. (2002) Exp5 exports eEF1A via tRNA from nuclei and synergizes other transport pathways to confine translation to the cytoplasm. EMBO J. 21, 6205-6215
33. Llorens, F., Roher, N., Miro, F. A., Sarno, S., Ruiz, F. X., Meggio, F., Plana, M., Pinna, L. and Itarte, E. (2003) Eukaryotic translation initiation factor eIF2beta binds to protein kinase CK2: effects on CK2alpha activity. Biochem. J. 375, 623-631
34. Beullens, M., Vulsteke, V., Van Eynde, A., Jagiello, I., Stalmans, W. and Bollen, M. (2000) The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding. Biochem. J. 352, 651-658