Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase

Cell

Volumn 112, Issue 2, 2003, Pages 243-256

  Orlicky, Stephen ^a   Tang, Xiaojing ^a   Willems, Andrew ^a   Tyers, Mike ^a,b   Sicheri, Frank ^a,b  

^a MOUNT SINAI HOSPITAL   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLIN E; CYCLINE; LEUCINE; PROLINE; THREONINE; UBIQUITIN PROTEIN LIGASE;

ARTICLE; BINDING SITE; CELL CYCLE; CELL CYCLE S PHASE; CONTROLLED STUDY; CRYSTAL STRUCTURE; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL;

EID: 0037462424     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00034-5     Document Type: Article

References (48)

1. Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell. 86:1996;263-274.
2. Brunger A.T., Adams P.D., Clore G.M., Gros P., Grosse-Kuntsleve, Jiang R.W., Kuszewski J., Nilges M., Pannu N.S., Read R.J. Crystallography and NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921.
3. Carson M. Ribbons 2.0. J. Appl. Crystallgr. 24:1991;958-961.
4. Chi Y., Huddleston M.J., Zhang X., Young R.A., Annan R.S., Carr S.A., Deshaies R.J. Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinase. Genes Dev. 15:2001;1078-1092.
5. Cohen P. The regulation of protein function by multisite phosphorylation. a 25 year update Trends Biochem. Sci. 25:2000;596-601.
6. de La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276:1997;472-494.
7. Eck M.J., Pluskey S., Trub T., Harrison S.C., Shoelson S.E. Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2. Nature. 379:1996;277-280.
8. Endicott J.A., Noble M.E., Tucker J.A. Cyclin-dependent kinases. inhibition and substrate recognition Curr. Opin. Struct. Biol. 9:1999;738-744.
9. Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell. 91:1997;221-230.
10. Ferrell J.E. Tripping the switch fantastic. how a protein kinase cascade can convert graded inputs into switch-like outputs Trends Biochem. Sci. 21:1996;460-466.
11. Fulop V., Jones D.T. Beta propellers. structural rigidity and functional diversity Curr. Opin. Struct. Biol. 9:1999;715-721.
12. Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T., McKenna S., Ptak C., Glover M., Shaw G.S. Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structure. 9:2001;897-904.
13. Harper J.W. Protein destruction. adapting roles for Cks proteins Curr. Biol. 11:2001;R431-R435.
14. Harper J.W., Burton J.L., Solomon M.J. The anaphase-promoting complex. it's not just for mitosis any more Genes Dev. 16:2002;2179-2206.
15. Hershko A., Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67:1998;425-479.
16. Hsiung Y.G., Chang H.C., Pellequer J.L., La Valle R., Lanker S., Wittenberg C. F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat. Mol. Cell. Biol. 21:2001;2506-2520.
17. Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P. Structure of an E6AP-UbcH7 complex. insights into ubiquitination by the E2-E3 enzyme cascade Science. 286:1999;1321-1326.
18. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the localization of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
19. Kaelin W.G. Jr. Molecular basis of the VHL hereditary cancer syndrome. Nat. Rev. Cancer. 2:2002;673-682.
20. Keyomarsi K., Tucker S.L., Buchholz T.A., Callister M., Ding Y., Hortobagyi G.N., Bedrosian I., Knickerbocker C., Toyofuku W., Lowe M.et al. Cyclin E and survival in patients with breast cancer. N. Engl. J. Med. 347:2002;1566-1575.
21. Fbw7 ubiquitin ligase. Science. 294:2001;173-177.
22. Lai E.C. Protein degradation. four E3s for the notch pathway Curr. Biol. 12:2002;R74-R78.
23. Lengronne A., Schwob E. The yeast CDK inhibitor Sic1 prevents genomic instability by promoting replication origin licensing in late G1. Mol. Cell. 9:2002;1067-1078.
24. Mammen M., Choi S.-K., Whitesides G.M. Polyvalent interactions in biological systems. implications for design and use of multivalent ligands and inhibitors Angew. Chem. 37:1998;2754-2794.
25. CDC4 ubiquitin-ligase complex. Mol. Biol. Cell. 11:2000;915-927.
26. Miller R., Gallo S.M., Khalak H.G., Weeks C.M. SnB. crystal structure determination via Shake-and-Bake J. Appl. Crystallgr. 27:1994;613-621.
27. Moberg K.H., Bell D.W., Wahrer D.C., Haber D.A., Hariharan I.K. Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature. 413:2001;311-316.
28. Nash P., Tang X., Orlicky S., Chen Q., Gertler F.B., Mendenhall M.D., Sicheri F., Pawson T., Tyers M. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature. 414:2001;514-521.
29. Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
30. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
31. Patton E.E., Willems A.R., Tyers M. Combinatorial control in ubiquitin-dependent proteolysis. don't Skp the F box hypothesis Trends Genet. 14:1998;236-243.
32. Pickart C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70:2001;503-533.
33. Schulman B.A., Carrano A.C., Jeffrey P.D., Bowen Z., Kinnucan E.R., Finnin M.S., Elledge S.J., Harper J.W., Pagano M., Pavletich N.P. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature. 408:2000;381-386.
34. SIC1 controls the G1 to S transition in S. cerevisiae. Cell. 79:1994;233-244.
35. Selkoe D.J. Presenilin, Notch, and the genesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 98:2001;11039-11041.
36. Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W. F box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell. 91:1997;209-219.
37. Spruck C.H., Won K.A., Reed S.I. Deregulated cyclin E induces chromosome instability. Nature. 401:1999;297-300.
38. Spruck C.H., Strohmaier H., Sangfelt O., Muller H.M., Hubalek M., Muller-Holzner E., Marth C., Widschwendter M., Reed S.I. hCDC4 gene mutations in endometrial cancer. Cancer Res. 62:2002;4535-4539.
39. Strohmaier H., Spruck C.H., Kaiser P., Won K.A., Sangfelt O., Reed S.I. Human F box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature. 413:2001;316-322.
40. ter Haar E., Harrison S.C., Kirchhausen T. Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin. Proc. Natl. Acad. Sci. USA. 97:2000;1096-1100.
41. Varshavsky A. Naming a targeting signal. Cell. 64:1991;13-15.
42. Verdecia M.A., Bowman M.E., Lu K.P., Hunter T., Noel J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7:2000;639-643.
43. Verma R., Annan R.S., Huddleston M.J., Carr S.A., Reynard G., Deshaies R.J. Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase. Science. 278:1997;455-460.
44. Wolf D.A., McKeon F., Jackson P.K. F box/WD-repeat proteins Pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of Cdc18p. Curr. Biol. 9:1999;373-376.
45. Yaffe M.B., Elia A.E. Phosphoserine/threonine-binding domains. Curr. Opin. Cell Biol. 13:2001;131-138.
46. Yaffe M.B., Rittinger K., Volinia S., Caron P.R., Aitken A., Leffers H., Gamblin S.J., Smerdon S.J., Cantley L.C. The structural basis for 14-3-3:phosphopeptide binding specificity. Cell. 91:1997;961-971.
47. Zheng N., Wang P., Jeffrey P.D., Pavletich N.P. Structure of a c-Cbl-UbcH7 complex. RING domain function in ubiquitin-protein ligases Cell. 102:2000;533-539.
48. Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P., Chu C., Koepp D.M., Elledge S.J., Pagano M.et al. Structure of the Cul1-Rbx1-Skp1-Fbox-Skp2 SCF ubiquitin ligase complex. Nature. 416:2002;703-709.