Faculty of Veterinary Medicine, University Gadjah Mada, Yogyakarta, Indonesia.
IMPLICATION OF ANNEXIN 1 IN PHAGOCYTOSIS: EFFECTS OF N-TERMINAL DOMAIN DELETIONS AND POINT MUTATIONS OF THE PHOSPHORYLATION SITE SER-27
Article first published online: 2 JAN 2013
© The Author(s) Journal compilation © 2001 International Federation for Cell Biology
Cell Biology International
Volume 25, Issue 8, pages 809–813, August 2001
How to Cite
Kusumawati, A., Liautard, J.-P. and Widada, S. J. (2001), IMPLICATION OF ANNEXIN 1 IN PHAGOCYTOSIS: EFFECTS OF N-TERMINAL DOMAIN DELETIONS AND POINT MUTATIONS OF THE PHOSPHORYLATION SITE SER-27. Cell Biology International, 25: 809–813. doi: 10.1006/cbir.2000.0704
- Issue published online: 2 JAN 2013
- Article first published online: 2 JAN 2013
- Accepted 16 November 2000; Received 15 August 2000
- Cited By
- annexin 1;
Directed mutagenesis, in the form of deletions and point mutations, was used to investigate the regulatory importance of the N-terminal domain of annexin 1. Wild-type and mutant forms were fused to green fluorescent protein (GFP) to track their localization and introduced in to J-774A.1 cells by transfection. The fusion of annexin 1 to GFP at the N- or C-terminal end did not alter the cellular distribution or co-localization with phagosomes. The effects of mutations were determined according to these characteristics. The prominent effect resulted from S27E mutation which mimics the phosphorylated state of Ser-27. Although still retaining the granular structures in the cytoplasm, S27E annexin 1 failed to associate with the phagosomal protein complex. This suggests an essential regulatory role of the phosphorylation of residue 27 in annexin 1 function.