Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein

Autoren

Philipp Trojan
Sebastian Rausch
Andreas Gieβl
Clementine Klemm
Eberhard Krause
Alexander Pulvermüller
Uwe Wolfrum

DOI

10.1016/j.bbamcr.2008.01.006

ISSN

0167-4889

Ausgabe der Veröffentlichung

6

Zeitschrift

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Sprache

en

Paginierung

1248 - 1260

Datum der Veröffentlichung

2008

Status

Published

Herausgeber

Elsevier BV

Herausgeber URL

http://dx.doi.org/10.1016/j.bbamcr.2008.01.006

Datum der Datenerfassung

2021

Titel

Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein

Ausgabe der Zeitschrift

1783

Data source: Crossref

Abstract

Centrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells. Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein kinase mediating phosphorylation of Cen1p, Cen2p and Cen4p, but not Cen3p, at a specific target sequence. CK2 and ciliary centrins co-localize in the photoreceptor cilium. Direct binding of CK2 and centrins to ciliary microtubules may spatially integrate the enzyme-substrate specificity in the cilium. Kinetic light-scattering assays revealed decreased binding affinities of phosphorylated centrins to transducin. Furthermore, we show that this decrease is based on the reduction of Ca2+-binding affinities of centrins. Present data describe a novel regulatory mechanism of reciprocal regulation of stimulus dependent distribution of signaling molecules.

Addresses

Zell-und Matrixbiologie, Institut für Zoologie, Johannes Gutenberg-Universität Mainz, Müllerweg 6, D-55099 Mainz, Germany.

Autoren

Philipp Trojan
Sebastian Rausch
Andreas Giessl
Clementine Klemm
Eberhard Krause
Alexander Pulvermüller
Uwe Wolfrum

DOI

10.1016/j.bbamcr.2008.01.006

eISSN

1878-2434

Externe Identifier

PubMed Identifier: 18269917

Open access

false

ISSN

0006-3002

Ausgabe der Veröffentlichung

6

Zeitschrift

Biochimica et biophysica acta

Schlüsselwörter

Cilia
Microtubules
Animals
Mice, Inbred C57BL
Cattle
Mice
Rats
Rats, Sprague-Dawley
Calcium
Transducin
Casein Kinase II
Calcium-Binding Proteins
Chromosomal Proteins, Non-Histone
Microscopy, Immunoelectron
Fluorescent Antibody Technique, Indirect
Blotting, Western
Protein Binding
Substrate Specificity
Phosphorylation
Dark Adaptation
Light
Mass Spectrometry
Photoreceptor Cells, Vertebrate

Sprache

eng

Medium

Print-Electronic

Online publication date

2008

Paginierung

1248 - 1260

Datum der Veröffentlichung

2008

Status

Published

Datum der Datenerfassung

2008

Titel

Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

Sub types

Research Support, Non-U.S. Gov't
Journal Article

Ausgabe der Zeitschrift

1783

Data source: Europe PubMed Central

Abstract

Centrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells. Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein kinase mediating phosphorylation of Cen1p, Cen2p and Cen4p, but not Cen3p, at a specific target sequence. CK2 and ciliary centrins co-localize in the photoreceptor cilium. Direct binding of CK2 and centrins to ciliary microtubules may spatially integrate the enzyme-substrate specificity in the cilium. Kinetic light-scattering assays revealed decreased binding affinities of phosphorylated centrins to transducin. Furthermore, we show that this decrease is based on the reduction of Ca2+-binding affinities of centrins. Present data describe a novel regulatory mechanism of reciprocal regulation of stimulus dependent distribution of signaling molecules.

Date of acceptance

2008

Autoren

Philipp Trojan
Sebastian Rausch
Andreas Giessl
Clementine Klemm
Eberhard Krause
Alexander Pulvermüller
Uwe Wolfrum

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/18269917

DOI

10.1016/j.bbamcr.2008.01.006

ISSN

0006-3002

Ausgabe der Veröffentlichung

6

Zeitschrift

Biochim Biophys Acta

Schlüsselwörter

Animals
Blotting, Western
Calcium
Calcium-Binding Proteins
Casein Kinase II
Cattle
Chromosomal Proteins, Non-Histone
Cilia
Dark Adaptation
Fluorescent Antibody Technique, Indirect
Light
Mass Spectrometry
Mice
Mice, Inbred C57BL
Microscopy, Immunoelectron
Microtubules
Phosphorylation
Photoreceptor Cells, Vertebrate
Protein Binding
Rats
Rats, Sprague-Dawley
Substrate Specificity
Transducin

Sprache

eng

Country

Netherlands

Paginierung

1248 - 1260

PII

S0167-4889(08)00009-8

Datum der Veröffentlichung

2008

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

2008

Titel

Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.

Sub types

Journal Article
Research Support, Non-U.S. Gov't

Ausgabe der Zeitschrift

1783

Data source: PubMed

Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein

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