Adenylate kinase phosphotransfer communicates cellular energetic signals to ATP-sensitive potassium channels

Antonio J Carrasco; Petras P Dzeja; Alexey E Alekseev; Darko Pucar; Leonid V Zingman; M. Roselle Abraham; Denice Hodgson; Martin Bienengraeber; Michel Puceat; Edwin Janssen; Be Wieringa; Andre Terzic

doi:10.1073/pnas.121038198

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Adenylate kinase phosphotransfer communicates cellular energetic signals to ATP-sensitive potassium channels

Journal article

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Adenylate kinase phosphotransfer communicates cellular energetic signals to ATP-sensitive potassium channels

Antonio J Carrasco, Petras P Dzeja, Alexey E Alekseev, Darko Pucar, Leonid V Zingman, M. Roselle Abraham, Denice Hodgson, Martin Bienengraeber, Michel Puceat, Edwin Janssen, …

Proceedings of the National Academy of Sciences - PNAS, Vol.98(13), pp.7623-7628

06/19/2001

DOI: 10.1073/pnas.121038198

PMCID: PMC34718

PMID: 11390963

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Abstract

Transduction of energetic signals into membrane electrical events governs vital cellular functions, ranging from hormone secretion and cytoprotection to appetite control and hair growth. Central to the regulation of such diverse cellular processes are the metabolism sensing ATP-sensitive K + (K ATP ) channels. However, the mechanism that communicates metabolic signals and integrates cellular energetics with K ATP channel-dependent membrane excitability remains elusive. Here, we identify that the response of K ATP channels to metabolic challenge is regulated by adenylate kinase phosphotransfer. Adenylate kinase associates with the K ATP channel complex, anchoring cellular phosphotransfer networks and facilitating delivery of mitochondrial signals to the membrane environment. Deletion of the adenylate kinase gene compromised nucleotide exchange at the channel site and impeded communication between mitochondria and K ATP channels, rendering cellular metabolic sensing defective. Assigning a signal processing role to adenylate kinase identifies a phosphorelay mechanism essential for efficient coupling of cellular energetics with K ATP channels and associated functions.

Biological Sciences

Details

Title: Subtitle: Adenylate kinase phosphotransfer communicates cellular energetic signals to ATP-sensitive potassium channels
Creators: Antonio J Carrasco - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Petras P Dzeja - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Alexey E Alekseev - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Darko Pucar - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Leonid V Zingman - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
M. Roselle Abraham - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Denice Hodgson - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Martin Bienengraeber - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Michel Puceat - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Edwin Janssen - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Be Wieringa - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Andre Terzic - Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology, and Experimental Therapeutics, Mayo Clinic, Mayo Foundation, Guggenheim 7, 200 First Street Southwest, Rochester, MN 55905; and
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.98(13), pp.7623-7628
DOI: 10.1073/pnas.121038198
PMID: 11390963
PMCID: PMC34718
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences
Language: English
Date published: 06/19/2001
Academic Unit: Roy J. Carver Department of Biomedical Engineering; Cardiovascular Medicine; Internal Medicine
Record Identifier: 9984094518802771

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