Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P21817 (
RyR1
)
1,154
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The present study documents the binding interaction of skeletal muscle sarcoplasmic reticulum (SR) transmembrane protein triadin with peripheral histidine-rich, Ca(2+)-binding protein (
HCP
). In addition to providing further evidence that
HCP
coenriches with
RyR1
, FKBP-12, triadin and calsequestrin (CS) in sucrose-density-purified TC vesicles, using specific polyclonal antibody, we show it to be expressed as a single protein species, both in fast-twitch and slow-twitch fibers, and to identically localize to the I-band. Colocalization of
HCP
and triadin at junctional triads is supported by the overlapping staining pattern using monoclonal antibodies to triadin. We show a specific binding interaction between digoxigenin-
HCP
and triadin, using ligand blot techniques. The importance of this finding is strengthened by the similarities in binding affinity and in Ca2+ dependence, (0.1-1 mM Ca2+) of the interaction of digoxigenin-
HCP
with immobilized TC vesicles. Suggesting that triadin dually interacts with
HCP
and with CS, at distinct sites, we have found that triadin-CS interaction in overlays does not require the presence of Ca2+. Consistent with the binding of CS to triadin luminal domain (Guo and Campbell, 1995), we show that binding sites for digoxigenin-CS, although not binding sites for digoxigenin-
HCP
, can be recovered in the 92 kDa triadin fragment, after chymotryptic cleavage of the NH2-terminal end of the folded molecule in intact TC vesicles. These differential effects form the basis for the hypothesis that
HCP
anchors to the junctional membrane domain of the SR, through binding to triadin short cytoplasmic domain at the NH2 terminus. Although the function of this interaction, as such, is not well understood, it seems of potential biological interest within the more general context of the structural-functional role of triadin at the triadic junction in skeletal muscle.
...
PMID:Interaction of triadin with histidine-rich Ca(2+)-binding protein at the triadic junction in skeletal muscle fibers. 1053 21