Homer Regulates Gain of Ryanodine Receptor Type 1 Channel Complex*
@article{Feng2002HomerRG, title={Homer Regulates Gain of Ryanodine Receptor Type 1 Channel Complex*}, author={Wei Feng and Jiancheng Tu and Tianzhong Yang and Patty S Vernon and Paul D. Allen and Paul F. Worley and Isaac N. Pessah}, journal={The Journal of Biological Chemistry}, year={2002}, volume={277}, pages={44722 - 44730} }
Homer proteins form an adapter system that regulates coupling of group 1 metabotropic glutamate receptors with intracellular inositol trisphosphate receptors and is modified by neuronal activity. Here, we demonstrate that Homer proteins also physically associate with ryanodine receptors type 1 (RyR1) and regulate gating responses to Ca2+, depolarization, and caffeine. In contrast to the prevailing notion of Homer function, Homer1c (long form) and Homer1-EVH1 (short form) evoke similar changes…
134 Citations
Homer Protein Increases Activation of Ca2+ Sparks in Permeabilized Skeletal Muscle*
- BiologyJournal of Biological Chemistry
- 2004
The results suggest that the EVH1 domain is critical for the agonist behavior on Ca2+ sparks and ryanodine binding, and that the coiled-coil domain, present in long but not short form Homer, confers an increase in agonist potential apparently through the multimeric association of Homer ligand.
Homer and the ryanodine receptor
- BiologyEuropean Biophysics Journal
- 2009
There are consensus sequences for Homer binding in the RyR and on many of the proteins that it interacts with in the massive RyR ion channel complex that also involve RyR channels.
Interaction of the Homer1 EVH1 domain and skeletal muscle ryanodine receptor.
- BiologyBiochemical and biophysical research communications
- 2019
In vitro modulation of the cardiac ryanodine receptor activity by Homer1
- BiologyPflügers Archiv - European Journal of Physiology
- 2009
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.
Homer proteins in Ca2+ signaling by excitable and non-excitable cells.
- Biology, ChemistryCell calcium
- 2007
Conditions associated with ER dysfunction activate homer 1a expression
- BiologyJournal of neurochemistry
- 2003
It is shown that homer 1a expression is induced in neuronal cell cultures under experimental conditions associated with ER dysfunction and may be activated by impairment of ER functioning just as it is by glutamate receptor activation.
Dynamic regulation of ryanodine receptor type 1 (RyR1) channel activity by Homer 1.
- BiologyCell calcium
- 2008
Homer Binds TRPC Family Channels and Is Required for Gating of TRPC1 by IP3 Receptors
- BiologyCell
- 2003
Vesl/Homer proteins regulate ryanodine receptor type 2 function and intracellular calcium signaling.
- BiologyCell calcium
- 2003
Homer2 Protein Regulates Plasma Membrane Ca2+-ATPase-mediated Ca2+ Signaling in Mouse Parotid Gland Acinar Cells*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2014
The role of Homer2 on Ca2+ signaling in parotid gland acinar cells using Homer2-deficient (Homer2−/−) mice is investigated and a Homer-binding PPXXF-like motif in the N terminus of PMCA that is required for interaction with Homer2 is identified.
References
SHOWING 1-10 OF 54 REFERENCES
Homer Regulates the Association of Group 1 Metabotropic Glutamate Receptors with Multivalent Complexes of Homer-Related, Synaptic Proteins
- BiologyNeuron
- 1998
Homer Binds a Novel Proline-Rich Motif and Links Group 1 Metabotropic Glutamate Receptors with IP3 Receptors
- BiologyNeuron
- 1998
Homer: a protein that selectively binds metabotropic glutamate receptors
- Biology, ChemistryNature
- 1997
A novel dendritic protein, Homer, is reported that contains a single, PDZ-like domain and binds specifically to the carboxy terminus of phosphoinositide-linked metabotropic glutamate receptors, suggesting that Homer mediates a novel cellular mechanism that regulates glutamate signalling.
Coupling of mGluR/Homer and PSD-95 Complexes by the Shank Family of Postsynaptic Density Proteins
- BiologyNeuron
- 1999
Transmembrane Redox Sensor of Ryanodine Receptor Complex*
- BiologyThe Journal of Biological Chemistry
- 2000
This study reveals the existence of a transmembrane redox sensor within the RyR1 channel complex that confers tight regulation of channel activity in response to changes in transmem BRO redox potential produced by cytoplasmic and luminal glutathione.
Enhanced dihydropyridine receptor channel activity in the presence of ryanodine receptor
- BiologyNature
- 1996
The results support the possibility of a retrograde signal by which RyR-1 enhances the function of DHPRs as Ca2+ channels, and measurements of charge movement indicate that the density ofDHPRs is similar in dyspedic and Ry R-1-expressing myotubes.
Divergent functional properties of ryanodine receptor types 1 and 3 expressed in a myogenic cell line.
- BiologyBiophysical journal
- 2000
Agonist-independent activation of metabotropic glutamate receptors by the intracellular protein Homer
- Biology, ChemistryNature
- 2001
In neurons, the constitutive activity of these receptors is controlled by Homer proteins, which bind directly to the receptors' carboxy-terminal intracellular domains, which show that these glutamate GPCRs can be directly activated by intraceocytes as well as by agonists.
Modulation of synaptic signalling complexes by Homer proteins
- BiologyJournal of neurochemistry
- 2002
This review will address primarily more recent studies on the regulation of Homer’1a expression and on the role of Homer/Vesl proteins in spine morphogenesis and receptor targeting and signalling.
Involvement of unique leucine-zipper motif of PSD-Zip45 (Homer 1c/vesl-1L) in group 1 metabotropic glutamate receptor clustering.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1999
It is demonstrated immunohistochemically that metabotropic glutamate receptor 1alpha and PSD-Zip45/Homer 1c are colocalized to synapses in the cerebellar molecular layer but not in the hippocampus, and the leucine zipper of subsynaptic scaffold protein is a candidate motif involved in neurotransmitter receptor clustering at the central synapse.