cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1

A Soren Leonard; Olena Yermolaieva; Alesia Hruska-Hageman; Candice C Askwith; Margaret P Price; John A Wemmie; Michael J Welsh

doi:10.1073/pnas.252782799

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cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1

Journal article

Open access

Peer reviewed

cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1

A Soren Leonard, Olena Yermolaieva, Alesia Hruska-Hageman, Candice C Askwith, Margaret P Price, John A Wemmie and Michael J Welsh

Proceedings of the National Academy of Sciences - PNAS, Vol.100(4), pp.2029-2034

02/18/2003

DOI: 10.1073/pnas.252782799

PMCID: PMC149953

PMID: 12578970

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Abstract

The acid-sensing ion channel-1 (ASIC1) contributes to synaptic plasticity and may influence the response to cerebral ischemia and acidosis. We found that cAMP-dependent protein kinase phosphorylated heterologously expressed ASIC1 and endogenous ASIC1 in brain slices. ASIC1 also showed significant phosphorylation under basal conditions. Previous studies showed that the extreme C-terminal residues of ASIC1 bind the PDZ domain of the protein interacting with C-kinase-1 (PICK1). We found that protein kinase A phosphorylation of Ser-479 in the ASIC1 C terminus interfered with PICK1 binding. In contrast, minimizing phosphorylation or mutating Ser-479 to Ala enhanced PICK1 binding. Phosphorylation-dependent disruption of PICK1 binding reduced the cellular colocalization of ASIC1 and PICK1. Thus, the ASIC1 C terminus contains two sites that influence its binding to PICK1. Regulation of this interaction by phosphorylation provides a mechanism to control the cellular localization of ASIC1.

Cyclic AMP-Dependent Protein Kinases - metabolism

Amino Acid Sequence

Phosphorylation

Acid Sensing Ion Channels

Mice, Inbred C57BL

Molecular Sequence Data

Nuclear Proteins - metabolism

Nerve Tissue Proteins

Hippocampus - cytology

Membrane Proteins

Hippocampus - metabolism

Animals

Carrier Proteins - metabolism

Sodium Channels - metabolism

Protein Binding

Mice

Neurons - metabolism

In Vitro Techniques

COS Cells

Details

Title: Subtitle: cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1
Creators: A Soren Leonard - Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, Howard Hughes Medical Institute, University of Iowa, Iowa City, IA 52242, USA
Olena Yermolaieva
Alesia Hruska-Hageman
Candice C Askwith
Margaret P Price
John A Wemmie
Michael J Welsh
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.100(4), pp.2029-2034
DOI: 10.1073/pnas.252782799
PMID: 12578970
PMCID: PMC149953
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences; United States
Grant note: DK25295 / NIDDK NIH HHS
Language: English
Date published: 02/18/2003
Academic Unit: Neurology; Molecular Physiology and Biophysics; Psychiatry; Iowa Neuroscience Institute; Neurosurgery; Internal Medicine
Record Identifier: 9984004077102771

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