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Conservation and divergence of Grb7 family of Ras-binding domains

Protein & Cell 2012年第1期3卷 60-70页

作者： Raju V.S.rajala ammaji rajala Vivek K.Gupta Department of Ophthalmology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Department of Cell Biology University of Oklahoma Health Sciences CenterOklahoma CityOK 73104USA Dean A.McGee Eye Institute Oklahoma CityOK 73104USA

Ras proteins are signal-transducing GTPases that cycle between inactive GDP-bound and active GTP-bound *** is a prolific signaling molecule interacting with a spectrum of effector molecules and acting through more than one signaling *** Ras-effector proteins contain a Ras-associating(RA)domain through which these associate with Ras in a GTP-dependent *** RA domain is highly conserved among the members of the growth factor receptor-bound(Grb)7 family of proteins which includes Grb7,Grb10 and *** laboratory has reported an unusual observation that RA domain of Grb14 binds to the C-terminal nucleotide binding site of cyclic nucleotide gated channel(CTRCNGA1)and inhibits the channel *** modeling of the CTR-CNGA1 displays 50%---70%tertiary structural similarity towards Ras *** named this region as Ras-like domain(RLD).The interaction between RA-Grb14 and RLD-CNGA1 is mediated through a simple protein-protein interaction temporally and spatially regulated by light and *** is interesting to note that Grb14 binds to GTPase-mutant Rab5,a Ras-related small GTPase whereas Grb10 binds only to GTP-bound form of active Rab5 but not to GTPase-defective mutant *** results suggest that Grb14 might have been evolved later in the evolution that binds to both Ras and nucleotide binding proteins such as *** studies also suggest that eukaryotic CNG channels could be evolved through a gene fusion between prokaryotic ion channels and cyclic nucleotide binding proteins,both of which might have undergone several sequence variations for functional adaptation during evolution.

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

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Neuroprotective role of protein tyrosine phosphatase-1B in rod photoreceptor neurons

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Protein & Cell 2013年第12期4卷 890-892页

作者： Raju V.S.rajala ammaji rajala Department of Ophthalmology University of Oklahoma Health Sciences CenterOklahoma CityOklahoma 73104USA Department of Physiology University of Oklahoma Health Sciences CenterOklahoma CityOklahoma 73104USA Department of Cell Biology University of Oklahoma Health Sciences CenterOklahoma CityOklahoma 73104USA Dean A.McGee Eye Institute Oklahoma CityOklahoma 73104USA

Dear Editor,Protein tyrosine phosphatase-1B(PT-P1B)is an abundant,widely expressed non-receptor tyrosine phosphatase,which is thought to be a key negative regulator of insulin signaling(Tonks,2003).Increased and prolo... 详细信息

关键词： PTP1B insulin of

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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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