Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-7-30
pubmed:abstractText
Cellular signaling proteins such as metabotropic glutamate receptors, Shank, and different types of ion channels are physically linked by Vesl (VASP/Ena-related gene up-regulated during seizure and LTP)/Homer proteins [Curr. Opin. Neurobiol. 10 (2000) 370; Trends Neurosci. 23 (2000) 80; J. Cell Sci. 113 (2000) 1851]. Vesl/Homer proteins have also been implicated in differentiation and physiological adaptation processes [Nat. Neurosci. 4 (2001) 499; Nature 411 (2001) 962; Biochem. Biophys. Res. Commun. 279 (2000) 348]. Here we provide evidence that a Vesl/Homer subtype, Vesl-1L/Homer-1c (V-1L), reduces the function of the intracellular calcium channel ryanodine receptor type 2 (RyR2). In contrast, Vesl-1S/Homer-1a (V-1S) had no effect on RyR2 function but reversed the effects of V-1L. In live cells, in calcium release studies and in single-channel electrophysiological recordings of RyR2, V-1L reduced RyR2 activity. Important physiological functions and pharmacological properties of RyR2 are preserved in the presence of V-1L. Our findings demonstrate that a protein-protein interaction between V-1L and RyR2 is not only necessary for organizing the structure of intracellular calcium signaling proteins [Curr. Opin. Neurobiol. 10 (2000) 370; Trends Neurosci. 23(2000)80; J. Cell Sci. 113 (2000) 1851; Nat Neurosci. 4 (2001) 499; Nature 411 (2001) 962; Biochem. Biophys. Res. Commun. 279 (2000) 348; Nature 386 (1997) 284], but that V-1L also directly regulates RyR2 channel activity by changing its biophysical properties. Thereby it may control cellular calcium homeostasis. These observations suggest a novel mechanism for the regulation of RyR2 and calcium-dependent cellular functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1,2-bis(2-aminophenoxy)ethane..., http://linkedlifedata.com/resource/pubmed/chemical/Aniline Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Caffeine, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic ADP-Ribose, http://linkedlifedata.com/resource/pubmed/chemical/Dantrolene, http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Fluo-3, http://linkedlifedata.com/resource/pubmed/chemical/Homer protein, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms, http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine, http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release..., http://linkedlifedata.com/resource/pubmed/chemical/Xanthenes
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0143-4160
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12887973-Aniline Compounds, pubmed-meshheading:12887973-Animals, pubmed-meshheading:12887973-Binding Sites, pubmed-meshheading:12887973-Blotting, Western, pubmed-meshheading:12887973-CHO Cells, pubmed-meshheading:12887973-Caffeine, pubmed-meshheading:12887973-Calcium, pubmed-meshheading:12887973-Calcium Signaling, pubmed-meshheading:12887973-Carrier Proteins, pubmed-meshheading:12887973-Cricetinae, pubmed-meshheading:12887973-Cyclic ADP-Ribose, pubmed-meshheading:12887973-Dantrolene, pubmed-meshheading:12887973-Dose-Response Relationship, Drug, pubmed-meshheading:12887973-Egtazic Acid, pubmed-meshheading:12887973-Electrophysiology, pubmed-meshheading:12887973-Microscopy, Fluorescence, pubmed-meshheading:12887973-Myocardium, pubmed-meshheading:12887973-Neuropeptides, pubmed-meshheading:12887973-Protein Binding, pubmed-meshheading:12887973-Protein Isoforms, pubmed-meshheading:12887973-Rats, pubmed-meshheading:12887973-Ryanodine, pubmed-meshheading:12887973-Ryanodine Receptor Calcium Release Channel, pubmed-meshheading:12887973-Sarcoplasmic Reticulum, pubmed-meshheading:12887973-Transfection, pubmed-meshheading:12887973-Xanthenes
pubmed:year
2003
pubmed:articleTitle
Vesl/Homer proteins regulate ryanodine receptor type 2 function and intracellular calcium signaling.
pubmed:affiliation
Department of Pharmacology and Neuroscience, University of North Texas Health Science Center, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't