期刊
BIOCHEMISTRY
卷 47, 期 25, 页码 6590-6601出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi800394s
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资金
- NHLBI NIH HHS [HL 084584, R01 HL084584-01A2, R01 HL084584, HL070015, R15 HL070015] Funding Source: Medline
- NIDCD NIH HHS [DC005349, R01 DC005349-06, R01 DC005349] Funding Source: Medline
ROS-GC1 membrane guanylate cyclase is a Ca(2+) bimodal signal transduction switch. It is turned off by a rise in free Ca(2+) from nanomolar to the semicromolar range in the photoreceptor outer segments and the olfactory bulb neurons; by a similar rise in the bipolar and ganglion retinal neurons it is turned on. These opposite operational modes of the switch are specified by its Ca(2+) sensing devices, respectively termed GCAPs and CD-GCAPs. Neurocalcin delta is a CD-GCAP. In the present study, the neurocalcin delta-modulated site, V(837)-L(858), in ROS-GC1 has been mapped. The location and properties of this site are unique. It resides within the core domain of the catalytic module and does not require the alpha-helical dimerization domain structural element (amino acids 767-811) for activating the catalytic module. Contrary to the current beliefs, the catalytic module is intrinsically active; it is directly regulated by the neurocalcin delta-modulated Ca(2+) signal and is dimeric in nature. A fold recognition based model of the catalytic domain of ROS-GC1 was built, and neurocalcin delta docking simulations were carried out to define the three-dimensional features of the interacting domains of the two molecules. These findings define a new transduction model for the Ca(2+) signaling of ROS-GC1.
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