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Science 3 January 1992:
Vol. 255. no. 5040, pp. 85 - 87
DOI: 10.1126/science.1532457
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Articles

Science, Vol 255, Issue 5040, 85-87
Copyright © 1992 by American Association for the Advancement of Science

articles

Interaction of p107 with cyclin A independent of complex formation with viral oncoproteins

ME Ewen, B Faha, E Harlow, and DM Livingston

Dana-Farber Cancer Institute, Boston, MA 02115.

The p107 protein and the retinoblastoma protein (RB) both bind specifically to two viral oncoproteins, the SV40 T antigen (T) and adenoviral protein E1A (E1A). Like RB, p107 contains a segment (the pocket) that, alone, can bind specifically to T, E1A, and multiple cellular proteins. Cyclin A bound to the p107 pocket, but not the RB pocket. Although both pockets contain two, related collinear subsegments (A and B), the unique sequence in the p107 pocket that occupies the space between A and B is required for the interaction with cyclin A.


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Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins..
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Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein..
L Zhu, S van den Heuvel, K Helin, A Fattaey, M Ewen, D Livingston, N Dyson, and E Harlow (1993)
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Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4.
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E2F: a link between the Rb tumor suppressor protein and viral oncoproteins.
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Identification of a growth suppression domain within the retinoblastoma gene product..
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