Annexin VI: an intracellular target for ATP

• Autorzy: Bandorowicz-Pikula J. , Danieluk M. , Wrzosek A. , Bus R. , Buchet R. , Pikula S.
• Języki publikacji: EN

Abstrakty

EN

Annexin VI (AnxVI), an Ca2+- and phospholipid-binding protein, interacts in vitro with ATP in a calcium-dependent manner. Experimental evidence indicates that its nucleotide-binding domain which is localized in the C-terminal half of the protein differs structurally from ATP/GTP-binding motifs found in other nucleotide-binding proteins. The amino-acid residues of AnxVI directly involved in ATP binding have not been yet defined. Binding of ATP to AnxVI induces changes in the secondary and tertiary structures of protein, affecting the affinity of AnxVI for Ca2+ and, in consequence, influencing the Ca2+ -dependent activities of AnxVI: binding to F-actin and to membranous phospholipids, and self-association of the annexin molecules. These observations suggest that ATP is a functional ligand for AnxVI in vivo, and ATP-sensitive AnxVI may play the role of a factor coupling vesicular transport and calcium homeostasis to cellular metabolism.

Słowa kluczowe

EN

2-p-toluidinylnapthalene-6-sulphonate; 2'-O-[2,4,6-trinitrophenyl]adenosine 5'-triphosphate; cellular metabolism; in vitro; annexin VI; phospholipid-binding protein

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1999
• Tom: 46
• Numer: 3
• Opis fizyczny: p.801-812,fig.

Twórcy

autor

Bandorowicz-Pikula J.

• M.Nencki Institute of Experimental Biology, L.Pasteura 3, 02-093 Warsaw, Poland

autor

Danieluk M.

autor

Wrzosek A.

autor

Bus R.

autor

Buchet R.

autor

Pikula S.

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