Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 21, Pages 16258-16266Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.081562
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Funding
- German National Academic Foundation
- Ruhr University Research School
- Deutsche Forschungsgemeinschaft [SFB 642]
- Elsa U. Pardee Foundation
- CONCERN Foundation
- MRC [MC_U117570592] Funding Source: UKRI
- Medical Research Council [MC_U117570592] Funding Source: researchfish
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NORE1A is a Ras-binding protein that belongs to a group of tumor suppressors known as the Ras association domain family. Their growth- and tumor-suppressive function is assumed to be dependent on association with the microtubule cytoskeleton. However, a detailed understanding of this interplay is still missing. Here, we show that NORE1A directly interacts with tubulin and is capable of nucleating microtubules. Strikingly, the ability to stimulate nucleation is regulated in a dual specific way either via phosphorylation of NORE1A within the Ras-binding domain by Aurora A kinase or via binding to activated Ras. We also demonstrate that NORE1A mediates a negative effect of activated Ras on microtubule nucleation. On the basis of our results, we propose a novel regulatory network composed of the tumor suppressor NORE1A, the mitotic kinase Aurora A, the small GTPase Ras, and the microtubule cytoskeleton.
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