Growth factor receptor-bound protein 14: a new modulator of photoreceptor-specific cyclic-nucleotide-gated channel

Vivek K. Gupta; Ammaji Rajala; Roger J. Daly; Raju V. S. Rajala

doi:10.1038/embor.2010.142

Growth factor receptor-bound protein 14: a new modulator of photoreceptor-specific cyclic-nucleotide-gated channel

Vivek K. Gupta, Ammaji Rajala, Roger J. Daly, Raju V. S. Rajala

Research output: Contribution to journal › Article › peer-review

32 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	861-867
Number of pages	7
Journal	EMBO Reports
Volume	11
Issue number	11
DOIs	https://doi.org/10.1038/embor.2010.142
Publication status	Published - 2010
Externally published	Yes

Keywords

cyclic-nucleotide-gated channel
Grb14
photoreceptor cells
Ras-associating domain
tyrosine kinase signalling

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10.1038/embor.2010.142

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abstract = "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.",

keywords = "cyclic-nucleotide-gated channel, Grb14, photoreceptor cells, Ras-associating domain, tyrosine kinase signalling",

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AU - Rajala, Ammaji

AU - Daly, Roger J.

AU - Rajala, Raju V. S.

PY - 2010

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AB - 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.

KW - cyclic-nucleotide-gated channel

KW - Grb14

KW - photoreceptor cells

KW - Ras-associating domain

KW - tyrosine kinase signalling

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JO - EMBO Reports

JF - EMBO Reports

IS - 11

ER -

Growth factor receptor-bound protein 14: a new modulator of photoreceptor-specific cyclic-nucleotide-gated channel

Abstract

Keywords

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