Protein kinase C modulates light responses in Neurospora by regulating the blue light photoreceptor WC-1

被引:62
作者
Franchi, L
Fulci, V
Macino, G
机构
[1] Univ Roma La Sapienza, Inst Pasteur, Fdn Cenci Bolognetti,Sez Genet Mol, Dipartimento Biotecnol Cellulari Ematol, I-00161 Rome, Italy
[2] NYU, Dept Biol, New York, NY 10003 USA
关键词
D O I
10.1111/j.1365-2958.2005.04545.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Neurospora protein kinase C (NPKC) is a regulator of light responsive genes. We have studied the function of NPKC in light response by investigating its biochemical and functional interaction with the blue light photoreceptor white-collar 1 (WC-1), showing that activation of NPKC leads to a significant decrease in WC-1 protein levels. Furthermore, we show that WC-1 and NPKC interact in a light-regulated manner in vivo, and that protein kinase C (PKC) phosphorylates WC-1 in vitro. We designed dominant negative and constitutively active forms of PKC which are able to induce either a large increase of WC-1 protein level or a strong reduction respectively. Moreover, these changes in PKC activity result in an altered light response. As WC-1 is a key component of Neurospora circadian clock and regulates the clock oscillator component FRQ we investigated the effect of NPKC-mutated forms on FRQ levels. We show that changes in PKC activity affect FRQ levels and the robustness of the circadian clock. Together these data identify NPKC as a novel component of the Neurospora light signal transduction pathway that modulates the circadian clock.
引用
收藏
页码:334 / 345
页数:12
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