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Growth factor receptor‐bound protein 14: a new modulator of photoreceptor‐specific cyclic‐nucleotide‐gated channel
Author(s) -
Gupta Vivek K,
Rajala Ammaji,
Daly Roger J,
Rajala Raju V S
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.142
Subject(s) - protein subunit , microbiology and biotechnology , cyclic nucleotide gated ion channel , biology , cyclic nucleotide binding domain , guanosine , signal transducing adaptor protein , biochemistry , cyclic nucleotide , chemistry , biophysics , nucleotide , signal transduction , gene
Growth factor receptor‐bound protein 14 (Grb14) is an adaptor protein that is involved in receptor tyrosine kinase signalling. In this study, we report that Grb14 interacts with the rod photoreceptor‐specific cyclic‐nucleotide‐gated channel alpha subunit (CNGA1) and decreases its affinity for cyclic guanosine monophosphate. Channel modulation is controlled by direct binding of the Grb14 Ras‐associating domain with the carboxy‐terminal region of CNGA1. We observed that the channel remains open in Grb14 −/− mice that are exposed to light, suggesting that Grb14 is a normal physiological modulator of CNG channel function in vivo .

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