ArticleAmerican journal of physiology. Heart and circulatory physiology2009
SAP97 regulates Kir2.3 channels by multiple mechanisms.
Article in American journal of physiology. Heart and circulatory physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- The Kir2.1E299V mutation increases atrial fibrillation vulnerability while protecting the ventricles against arrhythmias in a mouse model of short QT syndrome type 3.Cardiovascular research · 2024Article
- Cardiac potassium inward rectifier Kir2: Review of structure, regulation, pharmacology, and arrhythmogenesis.Heart rhythm · 2021Review
- Abnormal myocardial expression of SAP97 is associated with arrhythmogenic risk.American journal of physiology. Heart and circulatory physiology · 2020Article
- Improved affinity at the cost of decreased specificity: a recurring theme in PDZ-peptide interactions.Scientific reports · 2016Article
- Nav1.5 N-terminal domain binding to α1-syntrophin increases membrane density of human Kir2.1, Kir2.2 and Nav1.5 channels.Cardiovascular research · 2016Article
- Role of connexins and pannexins in cardiovascular physiology.Cellular and molecular life sciences : CMLS · 2015Review
- Protein assemblies of sodium and inward rectifier potassium channels control cardiac excitability and arrhythmogenesis.American journal of physiology. Heart and circulatory physiology · 2015Review
- Synapse-associated protein 97 regulates the membrane properties of fast-spiking parvalbumin interneurons in the visual cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Cardiomyocyte ATP release through pannexin 1 aids in early fibroblast activation.American journal of physiology. Heart and circulatory physiology · 2012Article
- Dynamic reciprocity of sodium and potassium channel expression in a macromolecular complex controls cardiac excitability and arrhythmia.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Regulation of cardiac inward rectifier potassium current (I(K1)) by synapse-associated protein-97.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
We examined the impact of coexpressing the inwardly rectifying potassium channel, Kir2.3, with the scaffolding protein, synapse-associated protein (SAP) 97, and determined that coexpression of these proteins caused an approximately twofold increase in current density. A combination of techniques was used to determine if the SAP97-induced increase in Kir2.3 whole cell currents resulted from changes in the number of channels in the cell membrane, unitary channel conductance, or channel open probability. In the absence of SAP97, Kir2.3 was found predominantly in a cytoplasmic, vesicular compartment with relatively little Kir2.3 localized to the plasma membrane. The introduction of SAP97 caused a redistribution of Kir2.3, leading to prominent colocalization of Kir2.3 and SAP97 and a modest increase in cell surface Kir2.3. The median Kir2.3 single channel conductance in the absence of SAP97 was approximately 13 pS, whereas coexpression of SAP97 led to a wide distribution of channel events with three distinct peaks centered at 16, 29, and 42 pS. These changes occurred without altering channel open probability, current rectification properties, or pH sensitivity. Thus association of Kir2.3 with SAP97 in HEK293 cells increased channel cell surface expression and unitary channel conductance. However, changes in single channel conductance play the major role in determining whole cell currents in this model system. We further suggest that the SAP97 effect results from SAP97 binding to the Kir2.3 COOH-terminal domain and altering channel conformation.
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Registered trials
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