ArticlePflugers Archiv : European journal of physiology2009
In vitro modulation of the cardiac ryanodine receptor activity by Homer1.
Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Reciprocal Homer1a and Homer2 Isoform Expression Is a Key Mechanism for MuscleInternational journal of molecular sciences · 2021Article
- Homer1 (VesL-1) in the rat esophagus: focus on myenteric plexus and neuromuscular junction.Histochemistry and cell biology · 2017Article
- Cardiac Ryanodine Receptor (Ryr2)-mediated Calcium Signals Specifically Promote Glucose Oxidation via Pyruvate Dehydrogenase.The Journal of biological chemistry · 2016Article
- The role of Homer1b/c in neuronal apoptosis following LPS-induced neuroinflammation.Neurochemical research · 2015Article
- Ryanodine receptors.Skeletal muscle · 2011Article
- Regulation of store-operated channels by scaffold proteins in a431 cells.Acta naturae · 2010Article
- Minding the calcium store: Ryanodine receptor activation as a convergent mechanism of PCB toxicity.Pharmacology & therapeutics · 2010Review
- Homer and the ryanodine receptor.European biophysics journal : EBJ · 2009Review
- Role of ryanodine receptor subtypes in initiation and formation of calcium sparks in arterial smooth muscle: comparison with striated muscle.Journal of biomedicine & biotechnology · 2009Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Homer protein family allows clustering and/or functional modulation of many proteins from different calcium signalling complexes including those formed by the ryanodine receptor (RyR) Ca(2+) release channel in skeletal muscle and the heart. Homer1b/c and the cardiac RyR (RyR2) are strongly expressed in the heart and neurons where their interaction with each other may modulate Ca(2+) signalling. However, functional interactions between Homer1b and RyR2 have been poorly defined. Our preliminary data and similar consensus binding sites for Homer in RyR2 and skeletal RyR (RyR1) proteins, led to the hypothesis that Homer may similarly regulate both RyR isoforms. Single-channel and [(3)H]ryanodine binding data showed that RyR2 and RyR1 activity increased to a maximum with ~50-100 nM Homer1b and fell with Homer1b > 200 nM. Homer1b (50 nM) activated RyR2 and RyR1 at all cytosolic [Ca(2+)]; estimated EC(50) value of RyR2 diminished from ~2.8 microM Ca(2+) (control) to ~1.9 microM Ca(2+) in the presence of 50 nM Homer1b. Short Homer1 (lacking the coiled-coil multimerisation domain) and Homer1b similarly modulated RyR2, indicating an action through ligand binding, not mutimerisation. These actions of Homer were generally similar in RyR2 and RyR1. The strong functional interactions suggest that Homer1 is likely to be an endogenous modulator of RyR channels in the heart and neurons as well as in skeletal muscle.
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Registered trials
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