An ATPase/Helicase Complex Is an Essential Cofactor for Oncogenic Transformation by c-Myc
In: Molecular Cell, Jg. 5 (2000-02-01), S. 321-330
Online
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Zugriff:
The c-Myc transactivation domain was used to affinity purify tightly associated nuclear proteins. Two of these proteins were identified as TIP49 and a novel related protein called TIP48, both of which are highly conserved in evolution and contain ATPase/helicase motifs. TIP49 and TIP48 are complexed with c-Myc in vivo, and binding is dependent on a c-Myc domain essential for oncogenic activity. A missense mutation in the TIP49 ATPase motif acts as a dominant inhibitor of c-Myc oncogenic activity but does not inhibit normal cell growth, indicating that functional TIP49 protein is an essential mediator of c-Myc oncogenic transformation. The TIP49 and TIP48 ATPase/helicase proteins represent a novel class of cofactors recruited by transcriptional activation domains that function in diverse pathways.
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An ATPase/Helicase Complex Is an Essential Cofactor for Oncogenic Transformation by c-Myc
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Autor/in / Beteiligte Person: | Cole, Michael D. ; McMahon, Steven B. ; Wood, Marcelo A. |
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Zeitschrift: | Molecular Cell, Jg. 5 (2000-02-01), S. 321-330 |
Veröffentlichung: | Elsevier BV, 2000 |
Medientyp: | unknown |
ISSN: | 1097-2765 (print) |
DOI: | 10.1016/s1097-2765(00)80427-x |
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