Retinoblastoma protein in growth suppression and death protection

Current Opinion in Genetics and Development

Volumn 7, Issue 1, 1997, Pages 39-45

  Wang, Jean Yj ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR E2F;

CANCER INHIBITION; CELL CYCLE S PHASE; CELL DEATH; CELL PROTECTION; CHEMICAL INTERACTION; GROWTH INHIBITION; MOUSE; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0031052563     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(97)80107-4     Document Type: Article

References (51)

1. 1/S regulation.
2. 1 restriction point regulation in Rb-deficient fibroblasts. Mol Cell Biol. 15:1996;2402-2407.
3. Du W, Vidal M, Xie J-E, Dyson N. RBF, a novel RB-related gene that regulates E2F activity and interacts with cyclin E in Drosophila. Genes Dev. 16:1996;1206-1218.
4. Beijersbergen RL, Bernards R. CEll cycle regulation by the retinoblastoma family of growth inhibitory proteins. Biochim Biophys Acta. 1287:1996;103-120.
5. Duronio RJ, O'Farrell PH, Xie JE, Brook A, Dyson N. The transcription factor E2F is required for S phase during Drosophila embryogenesis. Genes Dev. 9:1995;1445-1455.
6. Adams PD, Kaelin WG Jr. The cellular effects of E2F overexpression. Curr Top Microbiol Immun. 208:1996;79-93.
7. Ohtani K, DeGregori J, Nevins JR. Regulation of the cyclin E gene by transcription factor E2F1. Proc Natl Acad Sci USA. 92:1995;12146-12150.
8. Schulze A, Zerfass K, Spitkovsky D, Middendorp S, Berges J, Helin K, Jansen-Durr P, Henglein B. Cell cycle regulation of the cyclin A gene promoter is mediated by a variant E2F site. Proc Natl Acad Sci USA. 92:1995;11264-11268.
9. Pines J. Cyclins and cyclin-dependent kinases: theme and variations. Adv Cancer Res. 66:1995;181-212.
10. 1/S-regulatory genes. Mol Cell Biol. 15:1995;4215-4224.
11. Weintraub SJ, Prater CA, Dean DC. Retinoblastoma protein switches the E2F site from positive to negative element. Nature. 358:1992;259-261.
12. Weintraub SJ, Chow KNB, Luo RX, Zhang SH, He S, Dean DC. Mechanism of active transcriptional repression by the retinoblastoma protein. of special interest Nature. 375:1995;812-815 The authors of this report present evidence supporting the hypothesis that an important function of RB - E2F interaction is to target RB to specific promoters. Once recruited, RB can repress transcription by inhibiting other trans-activators (e.g. E1A, Elf-1, Pu.1) which contain the LXCXE motif for binding to the A/B domain of RB.
13. Wang JYJ, Knudsen ES, Welch PJ. The retinoblastoma tumor suppressor protein. Adv Cancer Res. 64:1994;25-85.
14. Bremner R, Cohen BL, Sopta M, Hamel PA, Ingles CJ, Gallie BL, Phillips RA. Direct transcriptional repression by pRB and its reversal by specific cyclins. of special interest Mol Cell Biol. 15:1995;3256-3265 This report presents evidence that RB has an E2F-independent transcription-repression function. Repression is observed with a RB - GAL4 fusion protein.
15. 1 phase of the cell cycle, when the b-myb gene is expressed. This result shows that the binding of E2F correlates with the suppression - but not the activation - of b-myb transcription. This is consistent with the hypothesis that an E2F-dependent DNA binding complex represses the b-myb promoter. Moreover, E2F binding to DNA must not be required for the transcription of b-myb.
16. Slansky JE, Farnham PJ. Introduction to the E2F family: protein structure and gene regulation. Curr Top Microbiol Immun. 208:1996;1-30.
17. Knudsen ES, Wang JYJ. Differential regulation of retinoblastoma protein function by specific cdk phosphorylation sites. J Biol Chem. 271:1996;8313-8320.
18. Field SJ, Tsai F-Y, Kuo F, Zubiaga AM, Kaelin WG Jr, Livingston DM, Orkin SH, Greenberg ME. E2F-1 functions in mice to promote apoptosis and suppress proliferation. of outstanding interest Cell. 85:1996;549-561 The authors describe the analyses of E2F-1-deficient mice, the emphasis being on thymocytes and T-cells. These studies reveal a physiological role of E2F in programmed cell death and in the suppression of tumor formation.
19. Yamasaki L, Jacks T, Bronson R, Goillot E, Harlow E, Dyson NJ. Tumor induction and tissue atrophy in mice lacking E2F-1. of outstanding interest Cell. 85:1996;537-548 This report describes the analyses of another line of E2F-1-deficient mice. A delayed onset of tumors was observed with E2F-1-deficient mice at older age. This observation indicates that E2F-1 has tumor-suppression function, a rather surprising finding given previous results that overproduction of E2F-1 can stimulate S phase entry and transform cultured cells. The biological function of E2F-1 my be highly dependent on the cell context and the developmental stages. Moreover, the oncogenic activity associated with the overproduction of E2F-1 may be caused by a more complex mechanism. The simple interpretation that E2F-1 has a growth-promoting function may have to be re-evaluated.
20. Sellers WR, Kaelin WG Jr. RB as a modulator of transcription. Biochem Biophys Acta. 1288:1996;1-5.
21. Kouzarides T. Transcriptional control by the retinoblastoma protein. Semin Cancer Biol. 6:1995;91-98.
22. Cavanaugh AH, Hempel WM, Taylor LJ, Rogalsky V, Todorov G, Rothblum LI. Activity of RNA polymerase I transcription factor UBF blocked by RB gene product. Nature. 374:1995;177-180.
23. White RJ, Trouche D, Martin K, Jackson SP, Kouzarides T. Repression of RNA polymerase III transcription by the retinoblastoma protein. Nature. 382:1996;88-90.
24. Shan B, Durfee T, Lee W-H. Disruption of RB/E2F-1 interaction by single point mutations in E2F-1 enhances S-phase entry and apoptosis. of special interest Proc Natl Acad Sci USA. 93:1996;679-684 A systematic analysis of the RB-binding site in E2F. This study led to the generation of E2F mutants which are defective in RB-binding but retain the ability to activate transcription. Overproduction of such E2F mutants is found to have enhanced biological in promoting S phase entry followed by cell death.
25. Welch PJ, Wang JYJ. Disruption of retinoblastoma protein function by coexpression of its C pocket fragment. of special interest Genes Dev. 9:1995;31-46 The authors demonstrate that RB can bind to E2F and c-Abl tyrosine kinase simultaneously in vitro as well as in vivo. This finding led to the proposal that RB has to assemble protein complexes to suppress cell growth. Supporting the proposed mechanism is the demonstration that co-expression of full-length RB with its fragments containing either the A/B domain or the C-region binding domains leads to the disruption of the growth-suppression function of RB.
26. Welch PJ, Wang JYJ. A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle. Cell. 75:1993;779-790.
27. Xiao Z-X, Chen J, Levine A, Modjtahedi N, Xing J, Sellers WR, Livingston DM. Interaction between the retinoblastoma protein and the oncoprotein MDM2. Nature. 375:1995;694-698.
28. Martin K, Trouche D, Hagemeier C, Sorensen TS, La Thangue NB, Kouzarides T. Stimulation of E2F1/DP1 transcriptional activity by MDM2 oncoprotein. Nature. 375:1995;691-694.
29. Muthukkumar S, Sells SF, Crist SA, Rangnekar VM. Interleukin-1 induces growth arrest by hypophosphorylation of the retinoblastoma susceptibility gene product RB. J Biol Chem. 271:1996;5733-5740.
30. 1/S progression.
31. Chow KNB, Dean DC. Domains A and B in the Rb pocket interact to form a transcriptional repressor motif. Mol Cell Biol. 16:1996;4862-4868.
32. Baskaran R, Chiang GG, Wang JYJ. Identification of a binding site in c-Abl tyrosine kinase for the C-terminal repeated domain of RNA polymerase II. Mol Cell Biol. 16:1996;3361-3369.
33. Kratzke RA, Otterson GA, Hogg A, Coxon AB, Geradts J, Cowell JK, Kaye FJ. Partial inactiavtion of the RB product in a family with incomplete penetrance of familial retinoblastoma and benign retinal tumors. Oncogene. 9:1994;1321-1326.
34. -/- cells are shown to be prone to DNA damage induced apoptosis.
35. Pan H, Griep AE. Altered cell cycle regulation in the lens of HPV-16 E6 or E7 transgenic mice: implications for tumor suppressor gene function in development. Genes Dev. 8:1994;1285-1299.
36. Slack RS, Skerjanc IS, Lach B, Craig J, Jardine K, McBurney MW. Cells differentiating into neuroectoderm undergo apoptosis in the absence of functional retinoblastoma family proteins. J Cell Biol. 129:1995;779-788.
37. Williams BO, Remington L, Albert DM, Mukai S, Bronson RT, Jacks T. Cooperative tumorigenic effects of germline mutations in Rb and p53. Nat Genet. 7:1994;480-484.
38. Harvey M, Vogel H, Lee EY-HP, Bradley A, Donehower LA. Mice deficient in both p53 and Rb develop tumors primarily of endocrine origin. Cancer Res. 55:1995;1146-1151.
39. Hiebert SW, Packham G, Strom DK, Haffner R, Oren M, Zambetti G, Cleveland JL. E2F-1 : DP-1 induces p53 and overrides survival factors to trigger apoptosis. of special interest Mol Cell Biol. 15:1995;6864-6874 This study was conducted using an interleukin-3-dependent murine myeloid cell line, 32D. The combined expression of E2F-1 and DP-1 can induce apoptosis in 32D cells even when interleukin-3 is present, suggesting that increased E2F activity can overcome survival factor signals to induce cell death. An increase in the steady-state levels of p53 is observed in the E2F-1/DP-1 overproducing cells, suggesting that E2F may activate p53 to induce death.
40. Martin SJ, Green DR. Protease activation during apoptosis: death by a thousand cuts. Cell. 82:1995;349-352.
41. White E. Life, death and the pursuit of apoptosis. Genes Dev. 10:1996;1-15.
42. Bing A, Dou QP. Cleavage of retinoblastoma protein during apoptosis: an interleukin 1 β-converting enzyme-like protease as candidate. Cancer Res. 56:1996;438-442.
43. -/- mice do not have developmental tumors, indicating that the loss of p107 does not increase tumor incidence whereas the loss of RB predisposes to tumor formation.
44. Cobrinik D, Lee M-H, Hannon G, Mulligan G, Bronson RT, Dyson N, Harlow E, Beach D, Weinberg RA, Jacks T. Shared role of the pRB-related p130 and p107 proteins in limb development. of special interest Genes Dev. 10:1996;1633-1644 Disruption of p107 or p130 alone does not cause any obvious defects in mice; however, the double-null mutants die soon after birth because they cannot breathe. The breathing defect is linked to excessive proliferation and the improper development of the rib cages which crush the lungs. This result demonstrates that p107 and p130 have redundant function in regulating cell proliferation and differentiation. Interestingly, mice with heterozygous mutation in p107 and homozygous mutation in p130 (and vice versa) do not develop tumors. This suggests that p107/p130 may not have tumor suppression function, despite their roles in the control of proliferation.
45. Grafi G, Burnett RJ, Helentjaris T, Larkins BA, DeCaprio JA, Sellers WR, Kaelin WG Jr. A maize cDNA encoding a member of the retinoblastoma protein family: involvement in endoreduplication. Proc Natl Acad Sci USA. 93:1996;8962-8967.
46. 1 transcriptional activators and the pRB family of proteins. Mol Cell Biol. 16:1996;1576-1583.
47. Singh P, Coe J, Hong W. A role for retinoblastoma protein in potentiating transcriptional activation by the glucocorticoid receptor. of special interest Nature. 374:1995;562-565 This study established RB as having a stimulatory role in transcription. The enhancement of transcription is mediated through the hBRM/hBRG factors.
48. Chen P-L, Riley DJ, Chen-Kiang S, Lee W-H. Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6. Proc Natl Acad Sci USA. 93:1996;465-469.
49. Johnson EM, Chen P-L, Krachmarov CP, Barr SM, Kanovsky M, Ma Z-W, Lee W-H. Association of human Pur-α with the retinoblastoma protein, Rb, regulates binding to the single-stranded DNA Pur-α recognition element. J Biol Chem. 270:1995;24352-24360.
50. Udvadia AJ, Templeton DJ, Horowitz JM. Functional interactions between the Retinoblastoma (Rb) protein and Sp-family members: superactivation by Rb requires amino acids necessary for growth suppression. Proc Natl Acad Sci USA. 92:1995;3953-3957.
51. Shao Z, Ruppert S, Robbins PD. The Retinoblastoma-susceptibility gene product binds directly to the human TATA-binding protein-associated factor TAFII250. Proc Natl Acad Sci USA. 92:1995;3115-3119.