Correction to: Mutational Analysis of Glycogen Synthase Kinase 3β Protein Kinase Together with Kinome-Wide Binding and Stability Studies Suggests Context-Dependent Recognition of Kinases by the Chaperone Heat Shock Protein 90 (Molecular and Cellular Biology, (2016), 36, 6, (1007-1018), 10.1128/MCB.01045-15);Mutational analysis of glycogen synthase kinase 3β protein kinase together with kinome-wide binding and stability studies suggests context-dependent recognition of kinases by the chaperone heat shock protein 90

Molecular and Cellular Biology

Volumn 36, Issue 6, 2016, Pages 1007-1018

  Jin, Jing ^a,d   Tian, Ruijun ^a,e   Pasculescu, Adrian ^a   Dai, Anna Yue ^a   Williton, Kelly ^a   Taylor, Lorne ^a,f   Savitski, Mikhail M ^b   Bantscheff, Marcus ^b   Woodgett, James R ^a,c   Pawson, Tony ^a,c   Colwill, Karen ^a  

^a MOUNT SINAI HOSPITAL   (Canada)

^b GLAXOSMITHKLINE   (United Kingdom)

^c UNIVERSITY OF TORONTO   (Canada)

^d NORTHWESTERN UNIVERSITY   (United States)

^e SOUTHERN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^f RESEARCH INSTITUTE OF THE MCGILL UNIVERSITY HEALTH CENTRE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BONE MORPHOGENETIC PROTEIN RECEPTOR 1A; BRUTON TYROSINE KINASE; CELL CYCLE PROTEIN 37; CHAPERONE; CHECKPOINT KINASE 1; EPHRIN RECEPTOR B3; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GLYCOGEN SYNTHASE KINASE 3BETA; HEAT SHOCK PROTEIN 90; JANUS KINASE 2; GLYCOGEN SYNTHASE KINASE 3; GSK3B PROTEIN, HUMAN; GSK3B PROTEIN, MOUSE; PROTEIN BINDING; PROTEIN KINASE;

AMINO ACID SEQUENCE; ARTICLE; AUTOPHOSPHORYLATION; CARCINOGENESIS; CONTROLLED STUDY; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; ISOTOPE LABELING; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; PROTEIN SYNTHESIS; PROTEOMICS; STABLE TRANSFECTION; WILD TYPE; ANIMAL; CELL LINE; GENETICS; HUMAN; METABOLISM; MOUSE; MUTATION;

ANIMALS; CELL LINE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 BETA; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MICE; MUTATION; PROTEIN BINDING; PROTEIN KINASES;

EID: 84960354396     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00051-16     Document Type: Erratum

References (40)

1. Caplan AJ, Mandal AK, Theodoraki MA. 2007. Molecular chaperones and protein kinase quality control. Trends Cell Biol 17:87-92. http://dx.doi.org/10.1016/j.tcb.2006.12.002.
2. Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, Karras GI, Lindquist S. 2012. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 150:987-1001. http://dx.doi.org/10.1016/j.cell.2012.06.047.
3. Citri A, Harari D, Shohat G, Ramakrishnan P, Gan J, Lavi S, Eisenstein M, Kimchi A, Wallach D, Pietrokovski S, Yarden Y. 2006. Hsp90 recognizes a common surface on client kinases. J Biol Chem 281:14361-14369. http://dx.doi.org/10.1074/jbc. M512613200.
4. Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L. 2001. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 276:3702-3708. http://dx.doi.org/10.1074/jbc. M006864200.
5. Xu W, Yuan X, Xiang Z, Mimnaugh E, Marcu M, Neckers L. 2005. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat Struct Mol Biol 12:120-126. http://dx.doi.org/10.1038/nsmb885.
6. Taipale M, Tucker G, Peng J, Krykbaeva I, Lin ZY, Larsen B, Choi H, Berger B, Gingras AC, Lindquist S. 2014. A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158:434-448. http://dx.doi.org/10.1016/j.cell.2014.05.039.
7. Polier S, Samant RS, Clarke PA, Workman P, Prodromou C, Pearl LH. 2013. ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system. Nat Chem Biol 9:307-312. http://dx.doi.org/10.1038/nchembio.1212.
8. Theodoraki MA, Kunjappu M, Sternberg DW, Caplan AJ. 2007. Akt shows variable sensitivity to an Hsp90 inhibitor depending on cell context. Exp Cell Res 313:3851-3858. http://dx.doi.org/10.1016/j.yexcr.2007.06.022.
9. Pearl LH. 2005. Hsp90 and Cdc37-a chaperone cancer conspiracy. Curr Opin Genet Dev 15:55-61. http://dx.doi.org/10.1016/j.gde.2004.12.011.
10. Garcia-Carbonero R, Carnero A, Paz-Ares L. 2013. Inhibition of HSP90 molecular chaperones: moving into the clinic. Lancet Oncol 14:e358-e369. http://dx.doi.org/10.1016/S1470-2045(13)70169-4.
11. Neckers L, Trepel JB. 2014. Stressing the development of small molecules targeting HSP90. Clin Cancer Res 20:275-277. http://dx.doi.org/10.1158/1078-0432.CCR-13-2571.
12. Kim YS, Alarcon SV, Lee S, Lee MJ, Giaccone G, Neckers L, Trepel JB. 2009. Update on Hsp90 inhibitors in clinical trial. Curr Top Med Chem 9:1479-1492. http://dx.doi.org/10.2174/156802609789895728.
13. Moulick K, Ahn JH, Zong H, Rodina A, Cerchietti L, Gomes DaGama EM, Caldas-Lopes E, Beebe K, Perna F, Hatzi K, Vu LP, Zhao X, Zatorska D, Taldone T, Smith-Jones P, Alpaugh M, Gross SS, Pillarsetty N, Ku T, Lewis JS, Larson SM, Levine R, Erdjument-Bromage H, Guzman ML, Nimer SD, Melnick A, Neckers L, Chiosis G. 2011. Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90. Nat Chem Biol 7:818-826. http://dx.doi.org/10.1038/nchembio.670.
14. Neckers L. 2006. Using natural product inhibitors to validate Hsp90 as a molecular target in cancer. Curr Top Med Chem 6:1163-1171. http://dx.doi.org/10.2174/156802606777811979.
15. Haupt A, Joberty G, BantscheffM, Frohlich H, Stehr H, Schweiger MR, Fischer A, Kerick M, Boerno ST, Dahl A, Lappe M, Lehrach H, Gonzalez C, Drewes G, Lange BM. 2012. Hsp90 inhibition differentially destabilises MAP kinase and TGF-beta signalling components in cancer cells revealed by kinase-targeted chemoproteomics. BMC Cancer 12:38. http://dx.doi.org/10.1186/1471-2407-12-38.
16. Kundrat L, Regan L. 2010. Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. Biochemistry 49: 7428-7438. http://dx.doi.org/10.1021/bi100386w.
17. So J, Pasculescu A, Dai AY, Williton K, James A, Nguyen V, Creixell P, Schoof EM, Sinclair J, Barrios-Rodiles M, Gu J, Krizus A, Williams R, Olhovsky M, Dennis JW, Wrana JL, Linding R, Jorgensen C, Pawson T, Colwill K. 2015. Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy. Sci Signal 8:rs3. http://dx.doi.org/10.1126/scisignal.2005700.
18. Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T. 2004. Proteomic, functional, and domainbased analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr Biol 14:1436-1450. http://dx.doi.org/10.1016/j.cub.2004.07.051.
19. BantscheffM, Eberhard D, Abraham Y, Bastuck S, Boesche M, Hobson S, Mathieson T, Perrin J, Raida M, Rau C, Reader V, Sweetman G, Bauer A, Bouwmeester T, Hopf C, Kruse U, Neubauer G, Ramsden N, Rick J, Kuster B, Drewes G. 2007. Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat Biotechnol 25:1035-1044. http://dx.doi.org/10.1038/nbt1328.
20. Tian R, Wang H, Gish GD, Petsalaki E, Pasculescu A, Shi Y, Mollenauer M, Bagshaw RD, Yosef N, Hunter T, Gingras AC, Weiss A, Pawson T. 2015. Combinatorial proteomic analysis of intercellular signaling applied to the CD28 T-cell costimulatory receptor. Proc Natl Acad Sci U S A 112:E1594-E1603. http://dx.doi.org/10.1073/pnas.1503286112.
21. 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. http://dx.doi.org/10.1038/nbt.1511.
22. Proia DA, Bates RC. 2014. Ganetespib and HSP90: translating preclinical hypotheses into clinical promise. Cancer Res 74:1294-1300. http://dx.doi.org/10.1158/0008-5472.CAN-13-3263.
23. Doble BW, Woodgett JR. 2003. GSK-3: tricks of the trade for a multitasking kinase. J Cell Sci 116:1175-1186. http://dx.doi.org/10.1242/jcs.00384.
24. Sato S, Fujita N, Tsuruo T. 2000. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad SciUSA97:10832-10837. http://dx.doi.org/10.1073/pnas.170276797.
25. Dajani R, Fraser E, Roe SM, Young N, Good V, Dale TC, Pearl LH. 2001. Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 105: 721-732. http://dx.doi.org/10.1016/S0092-8674(01)00374-9.
26. Hughes K, Nikolakaki E, Plyte SE, Totty NF, Woodgett JR. 1993. Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J 12:803-808.
27. Frame S, Cohen P, Biondi RM. 2001. A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol Cell 7:1321-1327. http://dx.doi.org/10.1016/S1097-2765(01)00253-2.
28. Bagatell R, Paine-Murrieta GD, Taylor CW, Pulcini EJ, Akinaga S, Benjamin IJ, Whitesell L. 2000. Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents. Clin Cancer Res 6:3312-3318.
29. Pasculescu A, Schoof EM, Creixell P, Zheng Y, Olhovsky M, Tian R, So J, Vanderlaan RD, Pawson T, Linding R, Colwill K. 2014. CoreFlow: a computational platform for integration, analysis and modeling of complex biological data. J Proteomics 100:167-173. http://dx.doi.org/10.1016/j.jprot.2014.01.023.
30. Duncan JS, Whittle MC, Nakamura K, Abell AN, Midland AA, Zawistowski JS, Johnson NL, Granger DA, Jordan NV, Darr DB, Usary J, Kuan PF, Smalley DM, Major B, He X, Hoadley KA, Zhou B, Sharpless NE, Perou CM, Kim WY, Gomez SM, Chen X, Jin J, Frye SV, Earp HS, Graves LM, Johnson GL. 2012. Dynamic repro-gramming of the kinome in response to targeted MEK inhibition in triple-negative breast cancer. Cell 149:307-321. http://dx.doi.org/10.1016/j.cell.2012.02.053.
31. Wu Z, Moghaddas Gholami A, Kuster B. 2012. Systematic identification of the HSP90 candidate regulated proteome. Mol Cell Proteomics 11: M111.016675.
32. Sherman MY, Gabai VL. 2015. Hsp70 in cancer: back to the future. Oncogene 34:4153-4161. http://dx.doi.org/10.1038/onc.2014.349.
33. Shao J, Prince T, Hartson SD, Matts RL. 2003. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem 278:38117-38120. http://dx.doi.org/10.1074/jbc. C300330200.
34. Slamon DJ, Leyland-Jones B, Shak S, Fuchs H, Paton V, Bajamonde A, Fleming T, Eiermann W, Wolter J, Pegram M, Baselga J, Norton L. 2001. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N Engl J Med 344:783-792. http://dx.doi.org/10.1056/NEJM200103153441101.
35. Heisermann GJ, Wiley HS, Walsh BJ, Ingraham HA, Fiol CJ, Gill GN. 1990. Mutational removal of the Thr669 and Ser671 phosphorylation sites alters substrate specificity and ligand-induced internalization of the epidermal growth factor receptor. J Biol Chem 265:12820-12827.
36. Wayne N, Mishra P, Bolon DN. 2011. Hsp90 and client protein maturation. Methods Mol Biol 787:33-44. http://dx.doi.org/10.1007/978-1-61779-295-3_3.
37. Genest O, Reidy M, Street TO, Hoskins JR, Camberg JL, Agard DA, Masison DC, Wickner S. 2013. Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. Mol Cell 49:464-473. http://dx.doi.org/10.1016/j.molcel.2012.11.017.
38. Lochhead PA, Kinstrie R, Sibbet G, Rawjee T, Morrice N, Cleghon V. 2006. A chaperone-dependent GSK3beta transitional intermediate mediates activation-loop autophosphorylation. Mol Cell 24:627-633. http://dx.doi.org/10.1016/j.molcel.2006.10.009.
39. Echeverría PC, Bernthaler A, Dupuis P, Mayer B, Picard D. 2011. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS One 6:e26044. http://dx.doi.org/10.1371/journal.pone.0026044.
40. Karagöz GE, Rudiger SG. 2015. Hsp90 interaction with clients. Trends Biochem Sci 40:117-125. http://dx.doi.org/10.1016/j.tibs.2014.12.002.