Modulation of the plasma membrane Ca2+ pump.
The plasma membrane calcium pump, which ejects Ca2+ from the cell, is regulated by calmodulin. In the absence of calmodulin, the pump is relatively inactive; binding of calmodulin to a specific domain stimulates its activity. Phosphorylation of the pump with protein kinase C or A may modify this regulation. Most of the regulatory functions of the enzyme are concentrated in a region at the carboxyl terminus. This region varies substantially between different isoforms of the pump, causing substantial differences in regulatory properties. The pump shares some motifs of the carboxyl terminus with otherwise unrelated proteins: The calmodulin-binding domain is a modified IQ motif (a motif which is present in myosins) and the last 3 residues of isoform 4b are a PDZ target domain. The pump is ubiquitous, with isoforms 1 and 4 of the pump being more widely distributed than 2 and 3. In some kinds of cells isoform 1 or 4 is missing, and is replaced by another isoform.
Penniston
J T
JT
Department of Biochemistry and Molecular Biology, Mayo Foundation, Rochester, MN 55905, USA.
Enyedi
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D000252:Calcium-Transporting ATPases / Q000502:physiology*; D002462:Cell Membrane / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D015398:Signal Transduction / Q000502:physiology*
D000252:Calcium-Transporting ATPases