In plant Ca(2+) pumps belonging to the P(2B) subfamily of P-type ATPases, the N-terminal cytoplasmic domain is responsible for pump autoinhibition. Binding of calmodulin (CaM) to this region results in pump activation but the structural basis for CaM activation is still not clear. All residues in a putative CaM-binding domain (Arg(43) to Lys(68)) were mutagenized and the resulting recombinant proteins were studied with respect to CaM binding and the activation state. The results demonstrate that (i) the binding site for CaM is overlapping with the autoinhibitory region and (ii) the autoinhibitory region comprises significantly fewer residues than the CaM-binding region. In a helical wheel projection of the CaM-binding domain, residues invol...
Calmodulin-like (CML) proteins are major EF hand-containing, calcium (Ca(2+))-binding proteins with ...
AbstractType IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppres...
The effect of phospholipids on the activity of isoform ACA8 of Arabidopsis thaliana plasma membrane ...
In plant Ca2+ pumps belonging to the P-2B subfamily of P-type ATPases, the N-terminal cytoplasmic do...
AbstractType IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppres...
ACA8 is a type 2B Ca2+-ATPase having a regulatory N terminus whose auto-inhibitory action can be sup...
Type 2B Ca2+-ATPases of plants (ACAs) have an extended cytosolic N-terminus containing an auto-inhib...
ACA8, a type 2B Ca ATPase, has a regulatory N-terminus with autoinhibitory action suppressed by bind...
The calcium ion (Ca2+) is essential for all plant and animal life. One important function of Ca2+ is...
The transport of calcium to the extracellular space carried out by plasma membrane Ca2+ pumps (PMCAs...
ACA8, a type 2B Ca ATPase, has a regulatory N-terminus with autoinhibitory action suppressed by bind...
AbstractPlant auto-inhibited Ca2+-ATPase 8 (ACA8) and animal plasma membrane Ca2+-ATPase 4b (PMCA4b)...
Type IIB Ca2+-ATPases have a terminal autoinhibitory, domain the action of which is suppressed by ca...
The transport of calcium to the extracellular space carried out by plasma membrane Ca2+ pumps (PMCAs...
AbstractIn plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regula...
Calmodulin-like (CML) proteins are major EF hand-containing, calcium (Ca(2+))-binding proteins with ...
AbstractType IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppres...
The effect of phospholipids on the activity of isoform ACA8 of Arabidopsis thaliana plasma membrane ...
In plant Ca2+ pumps belonging to the P-2B subfamily of P-type ATPases, the N-terminal cytoplasmic do...
AbstractType IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppres...
ACA8 is a type 2B Ca2+-ATPase having a regulatory N terminus whose auto-inhibitory action can be sup...
Type 2B Ca2+-ATPases of plants (ACAs) have an extended cytosolic N-terminus containing an auto-inhib...
ACA8, a type 2B Ca ATPase, has a regulatory N-terminus with autoinhibitory action suppressed by bind...
The calcium ion (Ca2+) is essential for all plant and animal life. One important function of Ca2+ is...
The transport of calcium to the extracellular space carried out by plasma membrane Ca2+ pumps (PMCAs...
ACA8, a type 2B Ca ATPase, has a regulatory N-terminus with autoinhibitory action suppressed by bind...
AbstractPlant auto-inhibited Ca2+-ATPase 8 (ACA8) and animal plasma membrane Ca2+-ATPase 4b (PMCA4b)...
Type IIB Ca2+-ATPases have a terminal autoinhibitory, domain the action of which is suppressed by ca...
The transport of calcium to the extracellular space carried out by plasma membrane Ca2+ pumps (PMCAs...
AbstractIn plant cells, the vacuole functions as a major calcium store. Although a calmodulin-regula...
Calmodulin-like (CML) proteins are major EF hand-containing, calcium (Ca(2+))-binding proteins with ...
AbstractType IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppres...
The effect of phospholipids on the activity of isoform ACA8 of Arabidopsis thaliana plasma membrane ...