Isolation of a novel visual-system-specific arrestin: an in vivo substrate for light-dependent phosphorylation

Harry LeVine; Dean P. Smith; Mike Whitney; Denise M. Malicki; Patrick J. Dolph; Gardiner F.H. Smith; Will Burkhart; Charles S. Zuker

doi:10.1016/0925-4773(90)90131-5

Isolation of a novel visual-system-specific arrestin: an in vivo substrate for light-dependent phosphorylation

Harry LeVine, Dean P. Smith, Mike Whitney, Denise M. Malicki, Patrick J. Dolph, Gardiner F.H. Smith, Will Burkhart, Charles S. Zuker

Molecular and Cellular Biochemistry

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

76 Scopus citations

Abstract

Absorption of a photon of light by rhodopsin triggers mechanisms responsible for excitation as well as regulation of the phototransduction cascade. Arrestins are a family of proteins that appear to be responsible for terminating the active state of G-protein-coupled receptors. One of the major substrates of light-dependent phosphorylation in the visual cascade of Drosophila was purified and partially sequenced. The complete primary structure of the protein was determined by isolating the corresponding gene, which revealed it to be a new isoform of arrestin, Arr2. Arr2 is 401 residues in length, and shares 47% sequence identity with the Drosophila Arr1 protein and 42% with human arrestin. We show that the two Drosophila arrestin genes are differentially regulated, and that Arr2 is a specific substrate for a calcium-dependent protein kinase. This is the first demonstration of in vivo regulation of arrestins in a transduction cascade, and provides a new level of modulation in the function of G-protein-coupled receptors.

Original language	English
Pages (from-to)	19-25
Number of pages	7
Journal	Mechanisms of Development
Volume	33
Issue number	1
DOIs	https://doi.org/10.1016/0925-4773(90)90131-5
State	Published - Dec 1990

Bibliographical note

Funding Information:
We thank Mike Socolich for his excellent help in chromosome squashes, and James Barbee for his help in the initial phase of this project. We also thank William Harris, Darwin Berg and members of the Zuker lab for their helpful comments. This work was supported by a grant from the NIH to C.S.Z. (P01 NS25916). D.P.S. is a NIH predoctoral trainee, D.M. is an MSTP trainee, and P.D. is supported by an NIH postdoctoral training grant in the visual sciences. C.S.Z. acknowledges support from the McKnight Endowment Fund for Neuroscience, the Pew Scholars Program in Biomedical Sciences, and The March of Dimes Basil O'Connor program. C.S.Z. is an investigator of the Howard Hughes Medical Institute.

Funding

We thank Mike Socolich for his excellent help in chromosome squashes, and James Barbee for his help in the initial phase of this project. We also thank William Harris, Darwin Berg and members of the Zuker lab for their helpful comments. This work was supported by a grant from the NIH to C.S.Z. (P01 NS25916). D.P.S. is a NIH predoctoral trainee, D.M. is an MSTP trainee, and P.D. is supported by an NIH postdoctoral training grant in the visual sciences. C.S.Z. acknowledges support from the McKnight Endowment Fund for Neuroscience, the Pew Scholars Program in Biomedical Sciences, and The March of Dimes Basil O'Connor program. C.S.Z. is an investigator of the Howard Hughes Medical Institute.

Funders	Funder number
UCI MSTP
March of Dimes Basil O'Connor program
National Institutes of Health (NIH)
National Institute of Neurological Disorders and Stroke	P01NS025916
McKnight Endowment Fund for Neuroscience

Keywords

Desensitization
G-protein coupled receptor
Phosphorylation
Phototransduction
Regulation

ASJC Scopus subject areas

Embryology
Developmental Biology

Access to Document

10.1016/0925-4773(90)90131-5

Cite this

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title = "Isolation of a novel visual-system-specific arrestin: an in vivo substrate for light-dependent phosphorylation",

abstract = "Absorption of a photon of light by rhodopsin triggers mechanisms responsible for excitation as well as regulation of the phototransduction cascade. Arrestins are a family of proteins that appear to be responsible for terminating the active state of G-protein-coupled receptors. One of the major substrates of light-dependent phosphorylation in the visual cascade of Drosophila was purified and partially sequenced. The complete primary structure of the protein was determined by isolating the corresponding gene, which revealed it to be a new isoform of arrestin, Arr2. Arr2 is 401 residues in length, and shares 47% sequence identity with the Drosophila Arr1 protein and 42% with human arrestin. We show that the two Drosophila arrestin genes are differentially regulated, and that Arr2 is a specific substrate for a calcium-dependent protein kinase. This is the first demonstration of in vivo regulation of arrestins in a transduction cascade, and provides a new level of modulation in the function of G-protein-coupled receptors.",

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author = "Harry LeVine and Smith, {Dean P.} and Mike Whitney and Malicki, {Denise M.} and Dolph, {Patrick J.} and Smith, {Gardiner F.H.} and Will Burkhart and Zuker, {Charles S.}",

note = "Funding Information: We thank Mike Socolich for his excellent help in chromosome squashes, and James Barbee for his help in the initial phase of this project. We also thank William Harris, Darwin Berg and members of the Zuker lab for their helpful comments. This work was supported by a grant from the NIH to C.S.Z. (P01 NS25916). D.P.S. is a NIH predoctoral trainee, D.M. is an MSTP trainee, and P.D. is supported by an NIH postdoctoral training grant in the visual sciences. C.S.Z. acknowledges support from the McKnight Endowment Fund for Neuroscience, the Pew Scholars Program in Biomedical Sciences, and The March of Dimes Basil O'Connor program. C.S.Z. is an investigator of the Howard Hughes Medical Institute.",

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AU - Smith, Dean P.

AU - Whitney, Mike

AU - Malicki, Denise M.

AU - Dolph, Patrick J.

AU - Smith, Gardiner F.H.

AU - Burkhart, Will

AU - Zuker, Charles S.

N1 - Funding Information: We thank Mike Socolich for his excellent help in chromosome squashes, and James Barbee for his help in the initial phase of this project. We also thank William Harris, Darwin Berg and members of the Zuker lab for their helpful comments. This work was supported by a grant from the NIH to C.S.Z. (P01 NS25916). D.P.S. is a NIH predoctoral trainee, D.M. is an MSTP trainee, and P.D. is supported by an NIH postdoctoral training grant in the visual sciences. C.S.Z. acknowledges support from the McKnight Endowment Fund for Neuroscience, the Pew Scholars Program in Biomedical Sciences, and The March of Dimes Basil O'Connor program. C.S.Z. is an investigator of the Howard Hughes Medical Institute.

PY - 1990/12

Y1 - 1990/12

N2 - Absorption of a photon of light by rhodopsin triggers mechanisms responsible for excitation as well as regulation of the phototransduction cascade. Arrestins are a family of proteins that appear to be responsible for terminating the active state of G-protein-coupled receptors. One of the major substrates of light-dependent phosphorylation in the visual cascade of Drosophila was purified and partially sequenced. The complete primary structure of the protein was determined by isolating the corresponding gene, which revealed it to be a new isoform of arrestin, Arr2. Arr2 is 401 residues in length, and shares 47% sequence identity with the Drosophila Arr1 protein and 42% with human arrestin. We show that the two Drosophila arrestin genes are differentially regulated, and that Arr2 is a specific substrate for a calcium-dependent protein kinase. This is the first demonstration of in vivo regulation of arrestins in a transduction cascade, and provides a new level of modulation in the function of G-protein-coupled receptors.

AB - Absorption of a photon of light by rhodopsin triggers mechanisms responsible for excitation as well as regulation of the phototransduction cascade. Arrestins are a family of proteins that appear to be responsible for terminating the active state of G-protein-coupled receptors. One of the major substrates of light-dependent phosphorylation in the visual cascade of Drosophila was purified and partially sequenced. The complete primary structure of the protein was determined by isolating the corresponding gene, which revealed it to be a new isoform of arrestin, Arr2. Arr2 is 401 residues in length, and shares 47% sequence identity with the Drosophila Arr1 protein and 42% with human arrestin. We show that the two Drosophila arrestin genes are differentially regulated, and that Arr2 is a specific substrate for a calcium-dependent protein kinase. This is the first demonstration of in vivo regulation of arrestins in a transduction cascade, and provides a new level of modulation in the function of G-protein-coupled receptors.

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Isolation of a novel visual-system-specific arrestin: an in vivo substrate for light-dependent phosphorylation

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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