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Annexin VI: an intracellular target for ATP.
- Source :
-
Acta biochimica Polonica [Acta Biochim Pol] 1999; Vol. 46 (3), pp. 801-12. - Publication Year :
- 1999
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Annexin A6 chemistry
Annexin A6 genetics
Binding Sites
Calcium metabolism
Cattle
Guanosine Triphosphate metabolism
Humans
In Vitro Techniques
Kinetics
Models, Molecular
Molecular Sequence Data
Nucleotides metabolism
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary
Adenosine Triphosphate metabolism
Annexin A6 metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0001-527X
- Volume :
- 46
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Acta biochimica Polonica
- Publication Type :
- Academic Journal
- Accession number :
- 10698288