Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM
10.1038/nsmb822
Crossref journal-article
Springer Science and Business Media LLC
Nature Structural & Molecular Biology (297)
Bibliography

Sengupta, J., Nilsson, J., Gursky, R., Spahn, C. M. T., Nissen, P., & Frank, J. (2004). Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM. Nature Structural & Molecular Biology, 11(10), 957–962.

Authors 6
  1. Jayati Sengupta (first)
  2. Jakob Nilsson (additional)
  3. Richard Gursky (additional)
  4. Christian M T Spahn (additional)
  5. Poul Nissen (additional)
  6. Joachim Frank (additional)
References 44 Referenced 214
  1. McCahill, A., Warwicker, J., Bolger, G.B., Houslay, M.D. & Yarwood, S.J. The RACK1 scaffold protein: a dynamic cog in cell response mechanisms. Mol. Pharmacol. 62, 1261–1273 (2002). (10.1124/mol.62.6.1261) / Mol. Pharmacol. by A McCahill (2002)
  2. Ron, D. et al. Cloning of an intracellular receptor for protein kinase C: a homolog of the β subunit of G proteins. Proc. Natl. Acad. Sci. USA 91, 839–843 (1994). (10.1073/pnas.91.3.839) / Proc. Natl. Acad. Sci. USA by D Ron (1994)
  3. Rodriguez, M.M., Ron, D., Touhara, K., Chen, C.H. & Mochly-Rosen, D. RACK1, a protein kinase C anchoring protein, coordinates the binding of activated protein kinase C and select pleckstrin homology domains in vitro. Biochemistry 38, 13787–13794 (1999). (10.1021/bi991055k) / Biochemistry by MM Rodriguez (1999)
  4. Chang, B.Y., Conroy, K.B., Machleder, E.M. & Cartwright, C.A. RACK1, a receptor for activated C kinase and a homolog of the β subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells. Mol. Cell. Biol. 18, 3245–3256 (1998). (10.1128/MCB.18.6.3245) / Mol. Cell. Biol. by BY Chang (1998)
  5. Chang, B.Y., Harte, R.A. & Cartwright, C.A. RACK1: a novel substrate for the Src protein-tyrosine kinase. Oncogene 21, 7619–7629 (2002). (10.1038/sj.onc.1206002) / Oncogene by BY Chang (2002)
  6. Liliental, J. & Chang, D.D. Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit. J. Biol. Chem. 273, 2379–2383 (1998). (10.1074/jbc.273.4.2379) / J. Biol. Chem. by J Liliental (1998)
  7. Yaka, R. et al. NMDA receptor function is regulated by the inhibitory scaffolding protein, RACK1. Proc. Natl. Acad. Sci. USA 99, 5710–5715 (2002). (10.1073/pnas.062046299) / Proc. Natl. Acad. Sci. USA by R Yaka (2002)
  8. Sondek, J. & Siderovski, D.P. Gγ-like (GGL) domains: new frontiers in G-protein signaling and β-propeller scaffolding. Biochem. Pharmacol. 61, 1329–1337 (2001). (10.1016/S0006-2952(01)00633-5) / Biochem. Pharmacol. by J Sondek (2001)
  9. Steele, M.R. et al. Identification of a surface on the β-propeller protein RACK1 that interacts with the cAMP-specific phosphodiesterase PDE4D5. Cell Signal. 13, 507–513 (2001). (10.1016/S0898-6568(01)00167-X) / Cell Signal. by MR Steele (2001)
  10. Link, A.J. et al. Direct analysis of protein complexes using mass spectrometry. Nat. Biotechnol. 17, 676–682 (1999). (10.1038/10890) / Nat. Biotechnol. by AJ Link (1999)
  11. Ceci, M. et al. Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Nature 426, 579–584 (2003). (10.1038/nature02160) / Nature by M Ceci (2003)
  12. Chantrel, Y., Gaisne, M., Lions, C. & Verdiere, J. The transcriptional regulator Hap1p (Cyp1p) is essential for anaerobic or heme-deficient growth of Saccharomyces cerevisiae: genetic and molecular characterization of an extragenic suppressor that encodes a WD repeat protein. Genetics 148, 559–569 (1998). (10.1093/genetics/148.2.559) / Genetics by Y Chantrel (1998)
  13. Shor, B., Calaycay, J., Rushbrook, J. & McLeod, M. Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe. J. Biol. Chem. 278, 49119–49128 (2003). (10.1074/jbc.M303968200) / J. Biol. Chem. by B Shor (2003)
  14. Inada, T. et al. One-step affinity purification of the yeast ribosome and its associated proteins and mRNAs. RNA 8, 948–958 (2002). (10.1017/S1355838202026018) / RNA by T Inada (2002)
  15. Baum, S., Bittins, M., Frey, S. & Seedorf, M. Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes. Biochem. J. 380, 823–830 (2004). (10.1042/bj20031962) / Biochem. J. by S Baum (2004)
  16. Angenstein, F. et al. A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons. J. Neurosci. 22, 8827–8837 (2002). (10.1523/JNEUROSCI.22-20-08827.2002) / J. Neurosci. by F Angenstein (2002)
  17. Li, A.M., Watson, A. & Fridovich-Keil, J.L. Scp160p associates with specific mRNAs in yeast. Nucleic Acids Res. 31, 1830–1837 (2003). (10.1093/nar/gkg284) / Nucleic Acids Res. by AM Li (2003)
  18. Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141–147 (2002). (10.1038/415141a) / Nature by AC Gavin (2002)
  19. Spahn, C.M. et al. Structure of the 80S ribosome from Saccharomyces cerevisiae—tRNA-ribosome and subunit-subunit interactions. Cell 107, 373–386 (2001). (10.1016/S0092-8674(01)00539-6) / Cell by CM Spahn (2001)
  20. Wimberly, B.T. et al. Structure of the 30S ribosomal subunit. Nature 407, 327–339 (2000). (10.1038/35030006) / Nature by BT Wimberly (2000)
  21. Brodersen, D.E., Clemons, W.M. Jr., Carter, A.P., Wimberly, B.T. & Ramakrishnan, V. Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA. J. Mol. Biol. 316, 725–768 (2002). (10.1006/jmbi.2001.5359) / J. Mol. Biol. by DE Brodersen (2002)
  22. Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190–199 (1996). (10.1006/jsbi.1996.0030) / J. Struct. Biol. by J Frank (1996)
  23. Spahn, C.M. et al. Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J. 23, 1008–1019 (2004). (10.1038/sj.emboj.7600102) / EMBO J. by CM Spahn (2004)
  24. Spahn, C.M. et al. Cryo-EM visualization of a viral internal ribosome entry site (IRES) bound to human 40S and 80S ribosomes: the IRES functions as an RNA-based translation factor. Cell 118, 465–475 (2004). (10.1016/j.cell.2004.08.001) / Cell by CM Spahn (2004)
  25. Morgan, D.G., Menetret, J.F., Neuhof, A., Rapoport, T.A. & Akey, C.W. Structure of the mammalian ribosome-channel complex at 17 Å resolution. J. Mol. Biol. 324, 871–886 (2002). (10.1016/S0022-2836(02)01111-7) / J. Mol. Biol. by DG Morgan (2002)
  26. Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808–814 (2004). (10.1038/nature02342) / Nature by M Halic (2004)
  27. Dube, P. et al. Correlation of the expansion segments in mammalian rRNA with the fine structure of the 80 S ribosome; a cryoelectron microscopic reconstruction of the rabbit reticulocyte ribosome at 21 Å resolution. J. Mol. Biol. 279, 403–421 (1998). (10.1006/jmbi.1998.1804) / J. Mol. Biol. by P Dube (1998)
  28. Bates, P.A., Kelley, L.A., MacCallum, R.M. & Sternberg, M.J. Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins 5 (suppl.), 39–46 (2001). (10.1002/prot.1168) / Proteins by PA Bates (2001)
  29. Lambright, D.G. et al. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311–319 (1996). (10.1038/379311a0) / Nature by DG Lambright (1996)
  30. Rath, B.K. et al. Fast 3D motif search of EM density maps using a locally normalized cross-correlation function. J. Struct. Biol. 144, 95–103 (2003). (10.1016/j.jsb.2003.09.029) / J. Struct. Biol. by BK Rath (2003)
  31. Bates, P.A. & Sternberg, M.J. Model building by comparison at CASP3: using expert knowledge and computer automation. Proteins 3 (suppl.), 47–54 (1999). (10.1002/(SICI)1097-0134(1999)37:3+<47::AID-PROT7>3.0.CO;2-F) / Proteins by PA Bates (1999)
  32. Chang, B.Y., Chiang, M. & Cartwright, C.A. The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. J. Biol. Chem. 276, 20346–20356 (2001). (10.1074/jbc.M101375200) / J. Biol. Chem. by BY Chang (2001)
  33. Chicurel, M.E., Singer, R.H., Meyer, C.J. & Ingber, D.E. Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. Nature 392, 730–733 (1998). (10.1038/33719) / Nature by ME Chicurel (1998)
  34. Steward, O. & Schuman, E.M. Compartmentalized synthesis and degradation of proteins in neurons. Neuron 40, 347–359 (2003). (10.1016/S0896-6273(03)00635-4) / Neuron by O Steward (2003)
  35. Shevchenko, A., Matthias, W., Ole, V. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850–858 (1996). (10.1021/ac950914h) / Anal. Chem. by A Shevchenko (1996)
  36. Keough, T., Lacey, M.P. & Youngquist, R.S. Derivatization procedures to facilitate de novo sequencing of lysine-terminated tryptic peptides using postsource decay matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 14, 2348–2356 (2000). (10.1002/1097-0231(20001230)14:24<2348::AID-RCM175>3.0.CO;2-8) / Rapid Commun. Mass Spectrom. by T Keough (2000)
  37. Sottrup-Jensen, L. A low-pH reverse-phase high-performance liquid chromatography system for analysis of the phenylthiohydantoins of S-carboxymethylcysteine and S-carboxyamidomethylcysteine. Anal. Biochem. 225, 187–188 (1995). (10.1006/abio.1995.1137) / Anal. Biochem. by L Sottrup-Jensen (1995)
  38. Wagenknecht, T., Grassucci, R. & Frank, J. Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli. J. Mol. Biol. 199, 137–147 (1988). (10.1016/0022-2836(88)90384-1) / J. Mol. Biol. by T Wagenknecht (1988)
  39. Frank, J., Penczek, P., Agrawal, R.K., Grassucci, R. & Heagle, A. Three-dimensional cryoelectron microscopy of ribosomes. Methods Enzymol. 317, 276–291 (2000). (10.1016/S0076-6879(00)17020-X) / Methods Enzymol. by J Frank (2000)
  40. Zhu, J., Penczek, P.A., Schröder, R. & Frank, J. Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs: procedure and application to the 70S Escherichia coli ribosome. J. Struct. Biol. 118, 197–219 (1997). (10.1006/jsbi.1997.3845) / J. Struct. Biol. by J Zhu (1997)
  41. Malhotra, A. et al. Escherichia coli 70 S ribosome at 15 Å resolution by cryo-electron microscopy: localization of fMet-tRNAfMet and fitting of L1 protein. J. Mol. Biol. 280, 103–116 (1998). (10.1006/jmbi.1998.1859) / J. Mol. Biol. by A Malhotra (1998)
  42. Gabashvili, I. et al. Solution structure of the E. coli 70S ribosome at 11.5 Å resolution. Cell 100, 537–549 (2000). (10.1016/S0092-8674(00)80690-X) / Cell by I Gabashvili (2000)
  43. Chothia, C. & Lesk, A.M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5, 823–826 (1986). (10.1002/j.1460-2075.1986.tb04288.x) / EMBO J. by C Chothia (1986)
  44. Carson, M. Ribbons 2.0. J. Appl. Crystallog. 24, 958–961 (1991). (10.1107/S0021889891007240) / J. Appl. Crystallog. by M Carson (1991)
Dates
Type When
Created 20 years, 11 months ago (Aug. 29, 2004, 1:45 p.m.)
Deposited 2 years, 3 months ago (May 19, 2023, 12:53 a.m.)
Indexed 1 month, 3 weeks ago (July 2, 2025, 3:08 p.m.)
Issued 20 years, 11 months ago (Aug. 29, 2004)
Published 20 years, 11 months ago (Aug. 29, 2004)
Published Online 20 years, 11 months ago (Aug. 29, 2004)
Published Print 20 years, 10 months ago (Oct. 1, 2004)
Funders 0

None

@article{Sengupta_2004, title={Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM}, volume={11}, ISSN={1545-9985}, url={http://dx.doi.org/10.1038/nsmb822}, DOI={10.1038/nsmb822}, number={10}, journal={Nature Structural &amp; Molecular Biology}, publisher={Springer Science and Business Media LLC}, author={Sengupta, Jayati and Nilsson, Jakob and Gursky, Richard and Spahn, Christian M T and Nissen, Poul and Frank, Joachim}, year={2004}, month=aug, pages={957–962} }