Nuclear association of tyrosine‐phosphorylated Vav to phospholipase C‐γ1 and phosphoinositide 3‐kinase during granulocytic differentiation of HL‐60 cells

FEBS Letters

Bertagnolo, Valeria²  Marchisio, Marco²  Capitani, Silvano²  Caramelli, Elisabetta¹  Volinia, Stefano³ 

[1] Institute of Histology and General Embryology, University of Bologna, Bologna, Italy;Signal Transduction Unit-Laboratory of Cell Biology, Section of Human Anatomy, Department of Morphology and Embryology, University of Ferrara, Ferrara, Italy;Section of Histology and Embryology, Department of Morphology and Embryology, University of Ferrara, Ferrara, Italy

关键词: Nucleus;    Phosphorylated protein;    Vav;    All-trans retinoic acid;    HL-60 cell;    PTK;    protein tyrosine kinase;    PI 3-K;    phosphoinositide 3-kinase;    PLC-γ1;    phospholipase C-γ1;    ATRA;    all-trans retinoic acid;   

DOI  :  10.1016/S0014-5793(98)01593-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The granulocytic differentiation of HL-60 cells induced by all-trans retinoic acid was accompanied by a progressive tyrosine phosphorylation of specific proteins in either cells or isolated nuclei. Among these phosphoproteins, we identified the Vav adaptor in whole cells as well as in the inner nuclear compartment, where the increase in its tyrosine phosphorylation level was more conspicuous. We also demonstrated the differentiation-dependent association of nuclear phosphorylated Vav to phospholipase C-γ1 and to the p85 regulatory subunit of phosphoinositide 3-kinase. The role of the Vav/phospholipase C-γ1/phosphoinositide 3-kinase phosphoprotein complexes in the nuclei of HL-60 induced to differentiate along the granulocytic lineage is discussed.

【 授权许可】

Unknown