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J. Biol. Chem., Vol. 276, Issue 20, 16998-17006, May 18, 2001

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The CK2 Phosphorylation of Vitronectin
PROMOTION OF CELL ADHESION VIA THE _v3-PHOSPHATIDYLINOSITOL 3-KINASE PATHWAY^*

Dalia Seger, Rony Seger, and Shmuel Shaltiel

From the Department of Biological Regulation, The Weizmann Institute of Science, Rehovot IL-76100, Israel

Phosphorylation of vitronectin (Vn) by casein kinase II was previously shown to occur at Thr⁵⁰ and Thr⁵⁷ and to augment a major physiological function of vitronectin-cell adhesion and spreading. Here we show that this phosphorylation increases cell adhesion via the _v3 (not via the _v5 integrin), suggesting that _v3 differs from _v5 in its biorecognition profile. Although both the phospho (CK2-PVn) and non-phospho (Vn) analogs of vitronectin (simulated by mutants Vn(T50E,T57E), and Vn(T50A,T57A), respectively) trigger the _v3 as well as the _v5 integrins, and equally activate the ERK pathway, these two forms are different in their activation of the focal adhesion kinase/phosphatidylinositol 3-kinase (PI3K)/protein kinase B (PKB) pathway. Specifically, we show (i) that, upon exposure of cells to Vn/CK2-PVn, their PKB activation depends on the availability of the _v3 integrin on their surface; (ii) that upon adhesion of the ₃-transfected cells onto the CK2-PVn, the extent of PKB activation coincides with the enhanced adhesion of these cells, and (iii) that both the PKB activation and the elevation in the adhesion of these cells is PI3K-dependent. The occurrence of a cell surface receptor that specifically distinguishes between a phosphorylated and a non-phosphorylated analog of Vn, together with the fact that it preferentially activates a distinct intra-cellular signaling pathway, suggest that extra-cellular CK2 phosphorylation may play an important role in the regulation of cell adhesion and migration.

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