Asc1p/RACK1 Connects Ribosomes to Eukaryotic Phosphosignaling

REFERENCES

• Coyle SM, Gilbert WV, Doudna JA. 2009. Direct link between RACK1 function and localization at the ribosome in vivo. Mol Cell Biol 29:1626–1634. https://doi.org/10.1128/MCB.01718-08.
   PubMed Web of Science ®Google Scholar
• Zeller CE, Parnell SC, Dohlman HG. 2007. The RACK1 ortholog Asc1 functions as a G-protein β subunit coupled to glucose responsiveness in yeast. J Biol Chem 282:25168–25176. https://doi.org/10.1074/jbc.M702569200.
   PubMedGoogle Scholar
• Breitkreutz A, Choi H, Sharom JR, Boucher L, Neduva V, Larsen B, Lin ZY, Breitkreutz BJ, Stark C, Liu G, Ahn J, Dewar-Darch D, Reguly T, Tang X, Almeida R, Qin ZS, Pawson T, Gingras AC, Nesvizhskii AI, Tyers M. 2010. A global protein kinase and phosphatase interaction network in yeast. Science 328:1043–1046. https://doi.org/10.1126/science.1176495.
   PubMed Web of Science ®Google Scholar
• Li JJ, Xie D. 2015. RACK1, a versatile hub in cancer. Oncogene 34:1890–1898. https://doi.org/10.1038/onc.2014.127.
   PubMed Web of Science ®Google Scholar
• Ceci M, Gaviraghi C, Gorrini C, Sala LA, Offenhauser N, Marchisio PC, Biffo S. 2003. Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Nature 426:579–584. https://doi.org/10.1038/nature02160.
   PubMed Web of Science ®Google Scholar
• Ruan Y, Sun L, Hao Y, Wang L, Xu J, Zhang W, Xie J, Guo L, Zhou L, Yun X, Zhu H, Shen A, Gu J. 2012. Ribosomal RACK1 promotes chemoresistance and growth in human hepatocellular carcinoma. J Clin Invest 122:2554–2566. https://doi.org/10.1172/JCI58488.
   PubMed Web of Science ®Google Scholar
• Gandin V, Gutierrez GJ, Brill LM, Varsano T, Feng Y, Aza-Blanc P, Au Q, McLaughlan S, Ferreira TA, Alain T, Sonenberg N, Topisirovic I, Ronai ZA. 2013. Degradation of newly synthesized polypeptides by ribosome-associated RACK1/c-Jun N-terminal kinase/eukaryotic elongation factor 1A2 complex. Mol Cell Biol 33:2510–2526. https://doi.org/10.1128/MCB.01362-12.
   PubMed Web of Science ®Google Scholar
• Hoffmann B, Mösch HU, Sattlegger E, Barthelmess IB, Hinnebusch A, Braus GH. 1999. The WD protein Cpc2p is required for repression of Gcn4 protein activity in yeast in the absence of amino-acid starvation. Mol Microbiol 31:807–822. https://doi.org/10.1046/j.1365-2958.1999.01219.x.
   PubMedGoogle Scholar
• Gerbasi VR, Weaver CM, Hill S, Friedman DB, Link AJ. 2004. Yeast Asc1p and mammalian RACK1 are functionally orthologous core 40S ribosomal proteins that repress gene expression. Mol Cell Biol 24:8276–8287. https://doi.org/10.1128/MCB.24.18.8276-8287.2004.
   PubMedGoogle Scholar
• Chiabudini M, Tais A, Zhang Y, Hayashi S, Wolfle T, Fitzke E, Rospert S. 2014. Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiae. Mol Cell Biol 34:4062–4076. https://doi.org/10.1128/MCB.00799-14.
   PubMedGoogle Scholar
• Thompson MK, Rojas-Duran MF, Gangaramani P, Gilbert WV. 2016. The ribosomal protein Asc1/RACK1 is required for efficient translation of short mRNAs. eLife 5: e11154. https://doi.org/10.7554/eLife.11154.
   Web of Science ®Google Scholar
• Kuroha K, Akamatsu M, Dimitrova L, Ito T, Kato Y, Shirahige K, Inada T. 2010. Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest. EMBO Rep 11:956–961. https://doi.org/10.1038/embor.2010.169.
   PubMedGoogle Scholar
• Matsuda R, Ikeuchi K, Nomura S, Inada T. 2014. Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast. Genes Cells 19:1–12. https://doi.org/10.1111/gtc.12106.
   PubMed Web of Science ®Google Scholar
• Wolf AS, Grayhack EJ. 2015. Asc1, homolog of human RACK1, prevents frameshifting in yeast by ribosomes stalled at CGA codon repeats. RNA 21:935–945. https://doi.org/10.1261/rna.049080.114.
   PubMed Web of Science ®Google Scholar
• Rachfall N, Schmitt K, Bandau S, Smolinski N, Ehrenreich A, Valerius O, Braus GH. 2013. RACK1/Asc1p, a ribosomal node in cellular signaling. Mol Cell Proteomics 12:87–105. https://doi.org/10.1074/mcp.M112.017277.
   PubMedGoogle Scholar
• Baum S, Bittins M, Frey S, Seedorf M. 2004. 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. https://doi.org/10.1042/bj20031962.
   PubMed Web of Science ®Google Scholar
• Ceci M, Welshhans K, Ciotti MT, Brandi R, Parisi C, Paoletti F, Pistillo L, Bassell GJ, Cattaneo A. 2012. RACK1 is a ribosome scaffold protein for β-actin mRNA/ZBP1 complex. PLoS One 7: e35034. https://doi.org/10.1371/journal.pone.0035034.
   Google Scholar
• Liu YV, Hubbi ME, Pan F, McDonald KR, Mansharamani M, Cole RN, Liu JO, Semenza GL. 2007. Calcineurin promotes hypoxia-inducible factor 1α expression by dephosphorylating RACK1 and blocking RACK1 dimerization. J Biol Chem 282:37064–37073. https://doi.org/10.1074/jbc.M705015200.
   PubMedGoogle Scholar
• Valerius O, Kleinschmidt M, Rachfall N, Schulze F, López Marín S, Hoppert M, Streckfuss-Bömeke K, Fischer C, Braus GH. 2007. The Saccharomyces homolog of mammalian RACK1, Cpc2/Asc1p, is required for FLO11-dependent adhesive growth and dimorphism. Mol Cell Proteomics 6:1968–1979. https://doi.org/10.1074/mcp.M700184-MCP200.
   PubMedGoogle Scholar
• Chang BY, Chiang M, Cartwright CA. 2001. 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. https://doi.org/10.1074/jbc.M101375200.
   PubMed Web of Science ®Google Scholar
• Kiely PA, O'Gorman D, Luong K, Ron D, O'Connor R. 2006. Insulin-like growth factor I controls a mutually exclusive association of RACK1 with protein phosphatase 2A and β1 integrin to promote cell migration. Mol Cell Biol 26:4041–4051. https://doi.org/10.1128/MCB.01868-05.
   PubMed Web of Science ®Google Scholar
• Urano D, Czarnecki O, Wang X, Jones AM, Chen JG. 2015. Arabidopsis receptor of activated C kinase1 phosphorylation by WITH NO LYSINE8 KINASE. Plant Physiol 167:507–516. https://doi.org/10.1104/pp.114.247460.
   PubMedGoogle Scholar
• Holt LJ, Tuch BB, Villen J, Johnson AD, Gygi SP, Morgan DO. 2009. Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325:1682–1686. https://doi.org/10.1126/science.1172867.
   PubMed Web of Science ®Google Scholar
• Smolka MB, Albuquerque CP, Chen SH, Zhou H. 2007. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc Natl Acad Sci U S A 104:10364–10369. https://doi.org/10.1073/pnas.0701622104.
   PubMed Web of Science ®Google Scholar
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. 2006. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635–648. https://doi.org/10.1016/j.cell.2006.09.026.
   PubMed Web of Science ®Google Scholar
• Olsen JV, Mann M. 2004. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc Natl Acad Sci U S A 101:13417–13422. https://doi.org/10.1073/pnas.0405549101.
   PubMed Web of Science ®Google Scholar
• Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. 2012. Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol Cell Proteomics 11:1510–1522. https://doi.org/10.1074/mcp.M112.017251.
   PubMed Web of Science ®Google Scholar
• Weinert BT, Scholz C, Wagner SA, Iesmantavicius V, Su D, Daniel JA, Choudhary C. 2013. Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep 4:842–851. https://doi.org/10.1016/j.celrep.2013.07.024.
   PubMed Web of Science ®Google Scholar
• Chasse SA, Flanary P, Parnell SC, Hao N, Cha JY, Siderovski DP, Dohlman HG. 2006. Genome-scale analysis reveals Sst2 as the principal regulator of mating pheromone signaling in the yeast Saccharomyces cerevisiae. Eukaryot Cell 5:330–346. https://doi.org/10.1128/EC.5.2.330-346.2006.
   PubMedGoogle Scholar
• Melamed D, Bar-Ziv L, Truzman Y, Arava Y. 2010. Asc1 supports cell-wall integrity near bud sites by a Pkc1 independent mechanism. PLoS One 5: e11389. https://doi.org/10.1371/journal.pone.0011389.
   Google Scholar
• Huang da W, Sherman BT, Lempicki RA. 2009. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc 4:44–57. https://doi.org/10.1038/nprot.2008.211.
   PubMed Web of Science ®Google Scholar
• Huang da W, Sherman BT, Lempicki RA. 2009. Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res 37:1–13. https://doi.org/10.1093/nar/gkn923.
   PubMed Web of Science ®Google Scholar
• Müller M, Kötter P, Behrendt C, Walter E, Scheckhuber CQ, Entian KD, Reichert AS. 2015. Synthetic quantitative array technology identifies the Ubp3-Bre5 deubiquitinase complex as a negative regulator of mitophagy. Cell Rep 10:1215–1225. https://doi.org/10.1016/j.celrep.2015.01.044.
   PubMed Web of Science ®Google Scholar
• Wilson-Grady JT, Ville J, Gygi SP. 2008. Phosphoproteome analysis of fission yeast. J Proteome Res 7:1088–1097. https://doi.org/10.1021/pr7006335.
   PubMed Web of Science ®Google Scholar
• Chang BY, Conroy KB, Machleder EM, Cartwright CA. 1998. 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. https://doi.org/10.1128/MCB.18.6.3245.
   PubMed Web of Science ®Google Scholar
• Sabila M, Kundu N, Smalls D, Ullah H. 2016. Tyrosine phosphorylation based homo-dimerization of Arabidopsis RACK1A proteins regulates oxidative stress signaling pathways in yeast. Front Plant Sci 7:176. https://doi.org/10.3389/fpls.2016.00176.
   PubMedGoogle Scholar
• Chang BY, Harte RA, Cartwright CA. 2002. RACK1: a novel substrate for the Src protein-tyrosine kinase. Oncogene 21:7619–7629. https://doi.org/10.1038/sj.onc.1206002.
   PubMed Web of Science ®Google Scholar
• Yatime L, Hein KL, Nilsson J, Nissen P. 2011. Structure of the RACK1 dimer from Saccharomyces cerevisiae. J Mol Biol 411:486–498. https://doi.org/10.1016/j.jmb.2011.06.017.
   PubMedGoogle Scholar
• Buchan DW, Minneci F, Nugent TC, Bryson K, Jones DT. 2013. Scalable web services for the PSIPRED protein analysis workbench. Nucleic Acids Res 41:W349–W357. https://doi.org/10.1093/nar/gkt381.
   PubMed Web of Science ®Google Scholar
• Jones DT. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 292:195–202. https://doi.org/10.1006/jmbi.1999.3091.
   PubMed Web of Science ®Google Scholar
• Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villen J. 2013. Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat Methods 10:676–682. https://doi.org/10.1038/nmeth.2519.
   PubMed Web of Science ®Google Scholar
• Ossareh-Nazari B, Bonizec M, Cohen M, Dokudovskaya S, Delalande F, Schaeffer C, Van Dorsselaer A, Dargemont C. 2010. Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required for ribophagy. EMBO Rep 11:548–554. https://doi.org/10.1038/embor.2010.74.
   PubMed Web of Science ®Google Scholar
• Lin J, Lee D, Choi Y, Lee SY. 2015. The scaffold protein RACK1 mediates the RANKL-dependent activation of p38 MAPK in osteoclast precursors. Sci Signal 8:ra54. https://doi.org/10.1126/scisignal.2005867.
   PubMedGoogle Scholar
• Belozerov VE, Ratkovic S, McNeill H, Hilliker AJ, McDermott JC. 2014. In vivo interaction proteomics reveal a novel p38 mitogen-activated protein kinase/Rack1 pathway regulating proteostasis in Drosophila muscle. Mol Cell Biol 34:474–484. https://doi.org/10.1128/MCB.00824-13.
   PubMedGoogle Scholar
• Lee CD, Tu BP. 2015. Glucose-regulated phosphorylation of the PUF protein Puf3 regulates the translational fate of its bound mRNAs and association with RNA granules. Cell Rep 11:1638–1650. https://doi.org/10.1016/j.celrep.2015.05.014.
   PubMed Web of Science ®Google Scholar
• Wu C, Lytvyn V, Thomas DY, Leberer E. 1997. The phosphorylation site for Ste20p-like protein kinases is essential for the function of myosin-I in yeast. J Biol Chem 272:30623–30626. https://doi.org/10.1074/jbc.272.49.30623.
   PubMedGoogle Scholar
• Booher RN, Deshaies RJ, Kirschner MW. 1993. Properties of Saccharomyces cerevisiae wee1 and its differential regulation of p34CDC28 in response to G1 and G2 cyclins. EMBO J 12:3417–3426.
   PubMed Web of Science ®Google Scholar
• Urban J, Soulard A, Huber A, Lippman S, Mukhopadhyay D, Deloche O, Wanke V, Anrather D, Ammerer G, Riezman H, Broach JR, De Virgilio C, Hall MN, Loewith R. 2007. Sch9 is a major target of TORC1 in Saccharomyces cerevisiae. Mol Cell 26:663–674. https://doi.org/10.1016/j.molcel.2007.04.020.
   PubMed Web of Science ®Google Scholar
• Schwartz D, Gygi SP. 2005. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat Biotechnol 23:1391–1398. https://doi.org/10.1038/nbt1146.
   PubMed Web of Science ®Google Scholar
• Chou MF, Schwartz D. 2011. Biological sequence motif discovery using motif-x. Curr Protoc Bioinformatics Chapter 13:13.15–13.24. https://doi.org/10.1002/0471250953.bi1315s35.
   Google Scholar
• Mok J, Kim PM, Lam HY, Piccirillo S, Zhou X, Jeschke GR, Sheridan DL, Parker SA, Desai V, Jwa M, Cameroni E, Niu H, Good M, Remenyi A, Ma JL, Sheu YJ, Sassi HE, Sopko R, Chan CS, De Virgilio C, Hollingsworth NM, Lim WA, Stern DF, Stillman B, Andrews BJ, Gerstein MB, Snyder M, Turk BE. 2010. Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci Signal 3:ra12. https://doi.org/10.1126/scisignal.2000482.
   PubMed Web of Science ®Google Scholar
• Gueldener U, Heinisch J, Koehler GJ, Voss D, Hegemann JH. 2002. A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res 30:e23. https://doi.org/10.1093/nar/30.6.e23.
   PubMed Web of Science ®Google Scholar
• Janke C, Magiera MM, Rathfelder N, Taxis C, Reber S, Maekawa H, Moreno-Borchart A, Doenges G, Schwob E, Schiebel E, Knop M. 2004. A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21:947–962. https://doi.org/10.1002/yea.1142.
   PubMed Web of Science ®Google Scholar
• Rivero-Gutierrez B, Anzola A, Martinez-Augustin O, de Medina FS. 2014. Stain-free detection as loading control alternative to Ponceau and housekeeping protein immunodetection in Western blotting. Anal Biochem 467:1–3. https://doi.org/10.1016/j.ab.2014.08.027.
   PubMed Web of Science ®Google Scholar
• Neumann B, Wu H, Hackmann A, Krebber H. 2016. Nuclear export of pre-ribosomal subunits requires Dbp5, but not as an RNA-helicase as for mRNA export. PLoS One 11:e0149571. https://doi.org/10.1371/journal.pone.0149571.
   PubMed Web of Science ®Google Scholar
• Cross FR, Tinkelenberg AH. 1991. A potential positive feedback loop controlling CLN1 and CLN2 gene expression at the start of the yeast cell cycle. Cell 65:875–883. https://doi.org/10.1016/0092-8674(91)90394-E.
   PubMedGoogle Scholar
• Kang D, Gho S, Suh M, Kang C. 2002. Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bull Korean Chem Soc 11:1511–1512.
   Google Scholar
• Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68:850–858. https://doi.org/10.1021/ac950914h.
   PubMed Web of Science ®Google Scholar
• Wiśniewski JR, Zougman A, Nagaraj N, Mann M. 2009. Universal sample preparation method for proteome analysis. Nat Methods 6:359–362. https://doi.org/10.1038/nmeth.1322.
   PubMed Web of Science ®Google Scholar
• Wessel D, Flügge UI. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 138:141–143. https://doi.org/10.1016/0003-2697(84)90782-6.
   PubMed Web of Science ®Google Scholar
• Mazanek M, Mituloviae G, Herzog F, Stingl C, Hutchins JR, Peters JM, Mechtler K. 2007. Titanium dioxide as a chemo-affinity solid phase in offline phosphopeptide chromatography prior to HPLC-MS/MS analysis. Nat Protoc 2:1059–1069. https://doi.org/10.1038/nprot.2006.280.
   PubMed Web of Science ®Google Scholar
• Kanshin E, Michnick SW, Thibault P. 2013. Displacement of N/Q-rich peptides on TiO2 beads enhances the depth and coverage of yeast phosphoproteome analyses. J Proteome Res 12:2905–2913. https://doi.org/10.1021/pr400198e.
   PubMed Web of Science ®Google Scholar
• Cox J, Mann M. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26:1367–1372. https://doi.org/10.1038/nbt.1511.
   PubMed Web of Science ®Google Scholar
• Ogur M, St John R, Nagai S. 1957. Tetrazolium overlay technique for population studies of respiration deficiency in yeast. Science 125:928–929. https://doi.org/10.1126/science.125.3254.928.
   PubMed Web of Science ®Google Scholar
• Vizcaino JA, Deutsch EW, Wang R, Csordas A, Reisinger F, Rios D, Dianes JA, Sun Z, Farrah T, Bandeira N, Binz PA, Xenarios I, Eisenacher M, Mayer G, Gatto L, Campos A, Chalkley RJ, Kraus HJ, Albar JP, Martinez-Bartolome S, Apweiler R, Omenn GS, Martens L, Jones AR, Hermjakob H. 2014. ProteomeXchange provides globally coordinated proteomics data submission and dissemination. Nat Biotechnol 32:223–226. https://doi.org/10.1038/nbt.2839.
   PubMed Web of Science ®Google Scholar
• Sengupta J, Nilsson J, Gursky R, Spahn CM, Nissen P, Frank J. 2004. Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM. Nat Struct Mol Biol 11:957–962. https://doi.org/10.1038/nsmb822.
   PubMed Web of Science ®Google Scholar
• Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M. 2011. The structure of the eukaryotic ribosome at 3.0 A resolution. Science 334:1524–1529. https://doi.org/10.1126/science.1212642.
   PubMed Web of Science ®Google Scholar
• Gnad F, de Godoy LM, Cox J, Neuhauser N, Ren S, Olsen JV, Mann M. 2009. High-accuracy identification and bioinformatic analysis of in vivo protein phosphorylation sites in yeast. Proteomics 9:4642–4652. https://doi.org/10.1002/pmic.200900144.
   PubMedGoogle Scholar
• Chi A, Huttenhower C, Geer LY, Coon JJ, Syka JE, Bai DL, Shabanowitz J, Burke DJ, Troyanskaya OG, Hunt DF. 2007. Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Proc Natl Acad Sci U S A 104:2193–2198. https://doi.org/10.1073/pnas.0607084104.
   PubMed Web of Science ®Google Scholar
• Zhao Y, Wang Q, Qiu G, Zhou S, Jing Z, Wang J, Wang W, Cao J, Han K, Cheng Q, Shen B, Chen Y, Zhang WJ, Ma Y, Zhang J. 2015. RACK1 promotes autophagy by enhancing the Atg14L-Beclin 1-Vps34-Vps15 complex formation upon phosphorylation by AMPK. Cell Rep 13:1407–1417. https://doi.org/10.1016/j.celrep.2015.10.011.
   PubMed Web of Science ®Google Scholar
• Kiely PA, Baillie GS, Barrett R, Buckley DA, Adams DR, Houslay MD, O'Connor R. 2009. Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase. J Biol Chem 284:20263–20274. https://doi.org/10.1074/jbc.M109.017640.
   PubMed Web of Science ®Google Scholar
• Ruiz Carrillo D, Chandrasekaran R, Nilsson M, Cornvik T, Liew CW, Tan SM, Lescar J. 2012. Structure of human Rack1 protein at a resolution of 2.45 A. Acta Crystallogr Sect F Struct Biol Cryst Commun 68:867–872. https://doi.org/10.1107/S1744309112027480.
   PubMedGoogle Scholar
• Ullah H, Scappini EL, Moon AF, Williams LV, Armstrong DL, Pedersen LC. 2008. Structure of a signal transduction regulator, RACK1, from Arabidopsis thaliana. Protein Sci 17:1771–1780. https://doi.org/10.1110/ps.035121.108.
   PubMedGoogle Scholar
• Stark C, Breitkreutz BJ, Reguly T, Boucher L, Breitkreutz A, Tyers M. 2006. BioGRID: a general repository for interaction datasets. Nucleic Acids Res 34:D535–D539. https://doi.org/10.1093/nar/gkj109.
   PubMed Web of Science ®Google Scholar