Dual mechanism of activation of plant plasma membrane Ca2+ ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps the calmodulin-binding site. (Articolo in rivista)

Type
Label
  • Dual mechanism of activation of plant plasma membrane Ca2+ ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps the calmodulin-binding site. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1080/09687680802508747 (literal)
Alternative label
  • Meneghelli S.; Fusca T.; Luoni L.; De Michelis M.I. (2008)
    Dual mechanism of activation of plant plasma membrane Ca2+ ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps the calmodulin-binding site.
    in Molecular membrane biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Meneghelli S.; Fusca T.; Luoni L.; De Michelis M.I. (literal)
Pagina inizio
  • 539 (literal)
Pagina fine
  • 546 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 25 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 6-7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopus (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biologia, Università di Milano, Istituto di Biofisica del CNR, Sezione di Milano, via G. Celoria 26, 20133 Milano, Italy (literal)
Titolo
  • Dual mechanism of activation of plant plasma membrane Ca2+ ATPase by acidic phospholipids: Evidence for a phospholipid binding site which overlaps the calmodulin-binding site. (literal)
Abstract
  • The effect of phospholipids on the activity of isoform ACA8 of Arabidopsis thaliana plasma membrane (PM) Ca2+-ATPase was evaluated in membranes isolated from Saccharomyces cerevisiae strain K616 expressing wild type or mutated ACA8 cDNA. Acidic phospholipids stimulated the basal Ca2+-ATPase activity in the following order of efficiency: phosphatidylinositol 4-monophosphate > phosphatidylserine > phosphatidylcholine approximately = phosphatidylethanolamine approximately = 0. Acidic phospholipids increased V(max-Ca2+) and lowered the value of K(0.5-Ca2+) below the value measured in the presence of calmodulin (CaM). In the presence of CaM acidic phospholipids activated ACA8 by further decreasing its K(0.5-Ca2+) value. Phosphatidylinositol 4-monophosphate and, with lower efficiency, phosphatidylserine bound peptides reproducing ACA8 N-terminus (aa 1-116). Single point mutation of three residues (A56, R59 and Y62) within the sequence A56-T63 lowered the apparent affinity of ACA8 for phosphatidylinositol 4-monophosphate by two to three fold, indicating that this region contains a binding site for acidic phospholipids. However, the N-deleted mutant Delta74-ACA8 was also activated by acidic phospholipids, indicating that acidic phospholipids activate ACA8 through a complex mechanism, involving interaction with different sites. The striking similarity between the response to acidic phospholipids of ACA8 and animal plasma membrane Ca2+-ATPase provides new evidence that type 2B Ca2+-ATPases share common regulatory properties independently of structural differences such as the localization of the terminal regulatory region at the N- or C-terminal end of the protein. (literal)
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