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Mechanism involved in the modulation of photoreceptor-specific cyclic nucleotidegated channel by the tyrosine kinase adapter protein Grb14

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Protein & Cell 2011年第11期2卷 906-917页

作者： Vivek k.Gupta Ammaji Rajala karla k.rodgers Raju V.S.Rajala Department of Ophthalmology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Department of Cell Biology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Department of Biochemistry and Molecular Biology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Dean A.McGee Eye Institute University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA

We recently found that growth factor receptor-bound(Grb)protein 14 is a novel physiological modulator of photoreceptor specific cyclic nucleotide-gated channel alpha subunit(CNGA1).Grb14 promotes the CNG channel closure through its Ras-associating(RA)*** the current study we show that this RA domain-mediated inhibition of rod CNG channel is electrostatic in ***14 competes with cGMP for the CNGA1 binding pocket and electrostatically interacts with Arg^(559) through a negatively chargedβ-turn at its RA ***,the three Glu residues(180–182)in Grb14 are absolutely critical for electrostatic interaction with the cGMP binding pocket and resultant *** study also demonstrates that substitution of Lys^(140) for Ala or in combination with polyglutamte mutants of Grb14 results in a significantly reduced binding with *** results suggest that in addition to Glu^(180–182) and Lys^(140),other residues in Grb14 may be involved in the electrostatic interaction with *** RA domain is highly conserved among the members of Grb7 family of proteins,which includes Grb7,Grb10 and ***,only Grb14 is able to modulate the channel activity,but not Grb7 and *** together,it suggests the existence of a divergence in RA domains among the members of the Grb7 family.

关键词： growth factor receptor-bound protein 14(Grb14) Ras-associating domain cyclic nucleotide gated channel rod outer segments tyrosine kinase signaling

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