ArticleThe Biochemical journal1995
In vivo and in vitro phosphorylation of annexin II in T cells: potential regulation by annexin V.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Review
- A conserved transcriptional program for MAIT cells across mammalian evolution.The Journal of experimental medicine · 2024Article
- Crucial role of Anxa2 in cancer progression: highlights on its novel regulatory mechanism.Cancer biology & medicine · 2019Article
- Article
- Annexin A2: its molecular regulation and cellular expression in cancer development.Disease markers · 2014Review
- Feedback regulation of endothelial cell surface plasmin generation by PKC-dependent phosphorylation of annexin A2.The Journal of biological chemistry · 2011Article
- Annexin 2 is not required for human immunodeficiency virus type 1 particle production but plays a cell type-dependent role in regulating infectivity.Journal of virology · 2010Article
- Regulation of nucleo-cytoplasmic shuttling of human annexin A2: a proposed mechanism.Molecular and cellular biochemistry · 2007Article
- Annexin V inhibits protein kinase C activity via a mechanism of phospholipid sequestration.The Biochemical journal · 1998Article
- Relocation of annexin V to platelet membranes is a phosphorylation-dependent process.The Biochemical journal · 1997Article
- RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes.The Journal of experimental medicine · 1997Article
- Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells.The Journal of cell biology · 1996Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to understand how signal transduction occurs during T cell activation, it is necessary to identify the key regulatory molecules whose function is influenced by phosphorylation. Annexins II (A-II) and V (A-V) belong to a large family of Ca(2+)-dependent phospholipid-binding proteins. Among many putative functions, annexins may be involved in signal transduction during cellular proliferation and differentiation. In the present study we show that A-II is phosphorylated in vivo in the Jurkat human T cell line. Indeed, A-II is phosphorylated after stimulation by phorbol myristate acetate and on serine residues after T cell antigen receptor (TcR) stimulation. In cytosol from Jurkat cells, A-II is phosphorylated only by Ca2+/phospholipid-stimulated kinases such as Ca(2+)-dependent protein kinases C (cPKCs). A-V inhibits the phosphorylation of A-II and other substrates of cPKCs and has no effect on kinases activated only by phospholipids. In conclusion, A-II is phosphorylated both in vitro and in vivo in Jurkat cells, and may play a role as a substrate during signal transduction in lymphocytes via the TcR through the PKC pathway. On the other hand, A-V could act as a potent modulator of cPKCs in Jurkat cells.
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