Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells

Akihiro Mizutani, Hiroshi Tokumitsu, Ryoji Kobayashi, Hiroyoshi Hidaka

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Annexin XI (CAP-50) is a probable target protein of calcyclin. Being different from other annexins, annexin XI localizes mainly in nuclei of cultured fibroblasts. In rat embryonic fibroblasts transformed by Rous sarcoma virus oncogene, SR-3Y1 cells, phosphorylation of annexin XI was increased on both serine and threonine residues (Ser <Thr), compared with findings in control 3Y1 cells. The amount of phosphorylated annexin XI was approximately 8.5% of the total cellular annexin XI and the phosphorylated annexin XI migrated slightly slower on SDS-polyacrylamide gel electrophoresis than did the non-phosphorylated form of annexin XI. Phosphorylated annexin XI was recovered in the cytoplasmic fraction and did not bind to phosphatidylserine vesicle in the presence of high Ca2+ (over 1 mM). Annexin XI was phosphorylated by mitogen-activated protein (MAP) kinase, which was reported to be activated in v-src-transformed fibroblast (Gupta, S. K., Gallego, C. Johnson, G. L. and Heasley, L. E. (1992) J. Biol. Chem. 267, 7987-7990), on both serine and threonine residues (Ser ≫ Thr) in vitro. Comparative phosphopeptide mappings analyzed by reverse-phase high performance liquid chromatography suggested that the sites phosphorylated in situ in SR-3Y1 cells are distinct from the sites by MAP kinase. Annexin XI phosphorylated by MAP kinase still possessed the ability to bind to phosphatidylserine vesicle. These results suggest that annexin XI is a substrate for some Ser/Thr kinase(s) which is activated in v-src-transformed cells and that the phosphorylation may regulate the function of annexin XI in living cells.

Original languageEnglish
Pages (from-to)15517-15522
Number of pages6
JournalJournal of Biological Chemistry
Volume268
Issue number21
Publication statusPublished - Jul 25 1993
Externally publishedYes

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Annexins
Phosphorylation
Fibroblasts
Mitogen-Activated Protein Kinases
Phosphatidylserines
Threonine
calcyclin-associated protein 50
Serine
Rous sarcoma virus
Phosphopeptides
High performance liquid chromatography
Reverse-Phase Chromatography
Electrophoresis
Viruses
Oncogenes
Rats
Polyacrylamide Gel Electrophoresis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mizutani, A., Tokumitsu, H., Kobayashi, R., & Hidaka, H. (1993). Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells. Journal of Biological Chemistry, 268(21), 15517-15522.

Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells. / Mizutani, Akihiro; Tokumitsu, Hiroshi; Kobayashi, Ryoji; Hidaka, Hiroyoshi.

In: Journal of Biological Chemistry, Vol. 268, No. 21, 25.07.1993, p. 15517-15522.

Research output: Contribution to journalArticle

Mizutani, A, Tokumitsu, H, Kobayashi, R & Hidaka, H 1993, 'Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells', Journal of Biological Chemistry, vol. 268, no. 21, pp. 15517-15522.
Mizutani A, Tokumitsu H, Kobayashi R, Hidaka H. Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells. Journal of Biological Chemistry. 1993 Jul 25;268(21):15517-15522.
Mizutani, Akihiro ; Tokumitsu, Hiroshi ; Kobayashi, Ryoji ; Hidaka, Hiroyoshi. / Phosphorylation of annexin XI (CAP-50) in SR-3Y1 cells. In: Journal of Biological Chemistry. 1993 ; Vol. 268, No. 21. pp. 15517-15522.
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