期刊
JOURNAL OF NEUROSCIENCE
卷 27, 期 3, 页码 604-615出版社
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.4099-06.2007
关键词
photoreceptor; pore; calcium channel; permeability; retinal degeneration; TRP channels; TRPC
资金
- Biotechnology and Biological Sciences Research Council [BB/D007585/1, E19850] Funding Source: Medline
- NEI NIH HHS [EY10852, R01 EY010852] Funding Source: Medline
- NHLBI NIH HHS [R01 HL083381, 1R01HL083381-01A1] Funding Source: Medline
- BBSRC [BB/D007585/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D007585/1, E19850] Funding Source: researchfish
Null mutations in the transient receptor potential (trp) gene eliminate the major, Ca2+-selective component of the light-sensitive conductance in Drosophila photoreceptors. Although it is the prototypical member of the TRP ion channel superfamily, conclusive evidence that TRP is a pore-forming channel subunit in vivo is lacking. We show here that mutating a specific acidic residue (Asp(621)) in the putative pore virtually eliminated Ca2+ permeation in vivo and altered other biophysical properties of the native TRP conductance. The results identify Asp621 as a critical residue of the TRP Ca2+ selectivity filter, provide the first rigorous demonstration that a TRP protein is a pore-forming subunit in any native system, and point to the likely location of the pore in mammalian canonical TRP channels. The specific elimination of Ca2+ permeation in TRP also provided a unique opportunity to address the roles of Ca2+ influx in vivo. We found that Asp621 mutations profoundly affected several key aspects of the light response and caused light-dependent retinal degeneration.
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