A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Hoyos, B., Imam, A., Chua, R., Swenson, C., Tong, G.X., Levi, E., Noy, N., Hammerling, U. (2000). The cysteine-rich regions of the regulatory domains of Raf and protein kinase C as retinoid receptors.  J. exp. Med. 192(6): 835--846. (Export to RIS)
FlyBase ID FBrf0132045
Publication Type Research paper
PubMed ID 10993914
PubMed Abstract Vitamin A and its biologically active derivatives, the retinoids, are recognized as key regulators of vertebrate development, cell growth, and differentiation. Although nuclear receptors have held the attention since their discovery a decade ago, we report here on serine/threonine kinases as a new class of retinoid receptors. The conserved cysteine-rich domain of the NH(2)-terminal regulatory domains of cRaf-1, as well as several select domains of the mammalian protein kinase C (PKC) isoforms alpha, delta, zeta, and mu, the Drosophila and yeast PKCs, were found to bind retinol with nanomolar affinity. The biological significance was revealed in the alternate redox activation pathway of these kinases. Retinol served as a cofactor to augment the activation of both cRaf and PKC alpha by reactive oxygen, whereas the classical receptor-mediated pathway was unaffected by the presence or absence of retinol. We propose that bound retinol, owing to its electron transfer capacity, functions as a tag to enable the efficient and directed redox activation of the cRaf and PKC families of kinases.
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Language of Publication English
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Publication Type Journal
Abbreviation J. exp. Med.
Title Journal of Experimental Medicine
Publication Year 1896-
ISBN/ISSN 0022-1007
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