FKBP12 associates tightly with the skeletal muscle type 1 ryanodine receptor, but not with other intracellular calcium release channels

Autor:	Vincenzo Sorrentino, John J. Mackrill, Mark Carmody, Cora O'Neill
Rok vydání:	2001
Předmět:	Cytoplasmic and Nuclear FK506 genetics/metabolism Skeletal muscle Receptors Cytoplasmic and Nuclear Tacrolimus Binding Protein 1A Biochemistry Ryanodine receptor 2 Inositol 1 4 5-trisphosphate receptor Calcium in biology chemistry.chemical_compound Structural Biology Receptors Inositol 1 4 5-Trisphosphate Receptors Protein Isoforms Inositol Cardiac muscle Receptor 5-Trisphosphate Receptors Glutathione Transferase Blotting Ryanodine receptor Calcineurin Brain Skeletal musculoskeletal system medicine.anatomical_structure cardiovascular system Muscle Rabbits Western medicine.medical_specialty Recombinant Fusion Proteins Blotting Western Biophysics Biology Tacrolimus Intracellular Ca2+ release channel Microsomes Internal medicine Genetics medicine Animals Muscle Skeletal Molecular Biology RYR1 Myocardium Cell Membrane Ryanodine Receptor Calcium Release Channel Cell Biology Animals Blotting Western Brain metabolism Calcineurin metabolism Calcium Channels metabolism Calcium metabolism Cell Membrane metabolism Glutathione Transferase genetics/metabolism Inositol 1 4 5-Trisphosphate Receptors Microsomes metabolism Muscle metabolism Myocardium metabolism Protein Isoforms Rabbits Receptors metabolism Recombinant Fusion Proteins genetics/metabolism Ryanodine Receptor Calcium Release Channel metabolism Tacrolimus Binding Protein 1A genetics/metabolism Tacrolimus metabolism Inositol 1 Endocrinology chemistry FKBP12 Calcium Calcium Channels
Zdroj:	FEBS Letters. 505:97-102
ISSN:	0014-5793
DOI:	10.1016/s0014-5793(01)02787-9
Popis:	This study compared the relative levels of ryanodine receptor (RyR) isoforms, inositol 1,4,5-trisphosphate receptor (IP3R) isoforms, and calcineurin, plus their association with FKBP12 in brain, skeletal and cardiac tissue. FKBP12 demonstrated a very tight, high affinity association with skeletal muscle microsomes, which was displaced by FK506. In contrast, FKBP12 was not tightly associated with brain or cardiac microsomes and did not require FK506 for removal from these organelles. Furthermore, of the proteins solubilised from skeletal muscle, cardiac muscle and brain microsomes, only skeletal muscle RyR1 bound to an FKBP12–glutathione-S-transferase fusion protein, in a high affinity FK506 displaceable manner. These results suggest that RyR1 has distinctive FKBP12 binding properties when compared to RyR2, RyR3, all IP3R isoforms and calcineurin.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52d17c00399a4e6e85befd24cc178124 https://doi.org/10.1016/s0014-5793(01)02787-9 Zobrazit plný text záznamu Plný text