Participation of annexins in protein phosphorylation

Abstract

Simultaneous discovery of members of the annexin family of calcium and phospholipid binding proteins by several groups is intimately linked to the possibility that these proteins may be controlled by phosphorylation. Indeed, annexin I and annexin II have been identified as major substrates for the tyrosine kinase activity associated with epidermal growth factor receptor (EGF-R) and for the retrovirus encoded protein tyrosine kinase pp60v-arc. Both annexins are also in vitro and/or in situ substrates for platelet derived growth factor (PDGF), insulin and hepatocyte growth factor/scatter factor (HGF/SF) receptor tyrosine kinases. In addition, to serve as substrates for tyrosine protein kinases some annexins are cellular targets for serine threonine protein kinases such as protein kinase C (PKC) and cAMP-dependent protein kinase A (PKA). Although the role of annexin phosphorylation has not been studied in detail, it is thought to influence their vesicle aggregation and phospholipid binding properties. Some annexins are also potent inhibitors of various serine/threonine and tyrosine kinases. The physiological functions of the annexins have still not been clearly defined. Therefore the identification of the ability of these proteins to undergo phosphorylation may be helpful in assigning them a precise biological role.

Metastable Macromolecular Complexes Containing High Mobility Group Nucleosome-binding Chromosomal Proteins in HeLa Nuclei

“…3C), were excised from the polyacrylamide gels and their tryptic peptides analyzed by MALDI-TOF. The results suggested that among the proteins specifically copurifying with HMGN1 were protein hnRNPA1 (30), hnRNPA2/B (30), and annexin II (31,32). Western analysis with specific antibodies confirmed that indeed hnRNPA1, but not hnRNPA2/B, was significantly enriched in the affinitybound proteins from cell extracts expressing the tagged HMGN proteins (Fig.…”

Identification of Novel Interaction between Annexin A2 and Keratin 17

“…Similarly, modulation of K17 steady-state levels causes change in the extent of AnxA2 association with the K17-rich filament pool and with AnxA2 phosphorylation. AnxA2 is a substrate of both Src and PKC (42), and is required for Src-dependent trafficking and Src-mediated transformation (43). Further, Src-mediated AnxA2 Y23 phosphorylation plays a role in cell scattering and branching morphogenesis by promoting actin cytoskeletal dynamics (44).…”

CCSP regulates cross talk between secretory cells and both ciliated cells and macrophages of the conducting airway

“…Phosphorylation of a tyrosine residue at position 21, NH 2 -terminal serine residues, and a COOH-terminal threonine residue, have been shown to be mediated through various receptor tyrosine kinases, PKC, or PKA, respectively (31,41,44). Modifications to the NH 2 -terminal domain influence calcium binding of ANXA1 and subsequently its ability to interact with plasma membranes and plasma membrane-associated EGF receptor (29,44).…”