Intracellular signaling through long-range linked functions in the Ca2+ transport ATPase.
The Ca2+ transport ATPases of intracellular membranes exhibit an intracellular long-range functional linkage which is the basic mechanistic device for Ca2+ transport through ATP utilization. The functional linkage operates between a phosphorylation (catalytic) domain located in the extramembranous region, and a Ca2+ binding domain located in the membrane bound region of the enzyme. The two domains are separated by a distance of approximately 50 A, and are both affected by binding of a single molecule of the highly specific inhibitor, thapsigargin, to the enzyme. Functional and structural features are here described to explain the long-range linkage through the protein structure.
Department of Biological Chemistry, School of Medicine, University of Maryland, Baltimore 21201.
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G
Inesi
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Z
Zhang
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Y
Sagara
M E
ME
Kirtley
D000595:Amino Acid Sequence; D000252:Calcium-Transporting ATPases / Q000502:physiology* / Q000648:ultrastructure*; D004721:Endoplasmic Reticulum / Q000201:enzymology / Q000648:ultrastructure; D007425:Intracellular Membranes / Q000201:enzymology* / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012519:Sarcoplasmic Reticulum / Q000201:enzymology / Q000648:ultrastructure; D015398:Signal Transduction / Q000502:physiology*
D000252:Calcium-Transporting ATPases