PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current

Alesia M Hruska-Hageman; Christopher J Benson; A Soren Leonard; Margaret P Price; Michael J Welsh

doi:10.1074/jbc.M405874200

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PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current

Journal article

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Peer reviewed

PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current

Alesia M Hruska-Hageman, Christopher J Benson, A Soren Leonard, Margaret P Price and Michael J Welsh

The Journal of biological chemistry, Vol.279(45), pp.46962-46968

11/05/2004

DOI: 10.1074/jbc.M405874200

PMID: 15317815

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Abstract

The acid-sensing ion channel-3 (ASIC3) is a degenerin/epithelial sodium channel expressed in the peripheral nervous system. Previous studies indicate that it participates in the response to mechanical and painful stimuli, perhaps contributing to mechanoreceptor and/or H+ -gated nociceptor function. ASIC3 subunits contain intracellular N and C termini that may control channel localization and function. We found that a PDZ-binding motif at the ASIC3 C terminus interacts with four different proteins that contain PDZ domains: PSD-95, Lin-7b, MAGI-1b, and PIST. ASIC3 and these interacting proteins were expressed in dorsal root ganglia and spinal cord, and PSD-95 co-precipitated ASIC3 from spinal cord. When expressed in heterologous cells, PSD-95 reduced the amplitude of ASIC3 acid-evoked currents, whereas Lin-7b increased current amplitude. PSD-95 and Lin-7b altered current density by decreasing or increasing, respectively, the amount of ASIC3 on the cell surface. The finding that multiple PDZ-containing proteins bind ASIC3 and can influence its presence in the plasma membrane suggests that they may play an important role in the contribution of ASIC3 to nociception and mechanosensation.

Disks Large Homolog 4 Protein

Protons

Immunoprecipitation

Humans

Electrophysiology

RNA, Messenger - metabolism

Tissue Distribution

Nerve Tissue Proteins - chemistry

Transfection

Membrane Proteins - physiology

Sodium Channels - metabolism

Cell Membrane - metabolism

Membrane Proteins - metabolism

CHO Cells

Protein Structure, Tertiary

Green Fluorescent Proteins - metabolism

Cricetinae

Nerve Tissue Proteins - physiology

Biotinylation

Acid Sensing Ion Channels

Intracellular Signaling Peptides and Proteins

Rats

DNA - metabolism

Reverse Transcriptase Polymerase Chain Reaction

Plasmids - metabolism

Rats, Sprague-Dawley

Amino Acid Motifs

Nerve Tissue Proteins - metabolism

Two-Hybrid System Techniques

Animals

Guanylate Kinases

Membrane Proteins - chemistry

Sodium Channels - chemistry

Protein Binding

Mice

COS Cells

Microscopy, Fluorescence

Ganglia, Spinal - metabolism

Hydrogen-Ion Concentration

Details

Title: Subtitle: PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current
Creators: Alesia M Hruska-Hageman - Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242, USA
Christopher J Benson
A Soren Leonard
Margaret P Price
Michael J Welsh
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.279(45), pp.46962-46968
DOI: 10.1074/jbc.M405874200
PMID: 15317815
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: DK54759 / NIDDK NIH HHS
Language: English
Date published: 11/05/2004
Academic Unit: Neurology; Molecular Physiology and Biophysics; Pulmonary, Critical Care, and Occupational Medicine; Cardiovascular Medicine; Fraternal Order of Eagles Diabetes Research Center; Neuroscience and Pharmacology; Neurosurgery; Internal Medicine
Record Identifier: 9984020490302771

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