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3. NPM-ALK Mediated Tyrosine Phosphorylation of ATP Citrate Lyase Regulates Lipid Metabolism and Promotes Oncogenesis of Anaplastic Large Cell Lymphoma

Author

Basappa, Johnvesly, primary, ElAzzouny, Mahmoud A, additional, Rolland, Delphine CM, additional, Velusamy, Thirunavukkarasu, additional, Hwang, Steven, additional, Basrur, Venkatesha, additional, Conlon, Kevin, additional, Zhao, Lili, additional, Bailey, Nathanael G., additional, Burant, Charles F, additional, Elenitoba-Johnson, Kojo SJ, additional, and Lim, Megan S, additional

Published
2015
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9. Aspirin Induces Platelet Apoptosis

Author

Zhao, Lili, primary, Zhang, Weilin, additional, Chen, Mengxing, additional, Zhang, Jiansheng, additional, Zhang, Mingyi, additional, Ruan, Changgeng, additional, and Dai, Kesheng, additional

Published
2012
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13. Ser559 of Glycoprotein Ibα Is Phosphorylated by Protein Kinase A Which Plays Key Roles In Regulating Von Willebrand Factor Binding, Surface Expression and Signaling of Glycoprotein Ib-IX

Author

Liao Yi, Changgeng Ruan, Liu Guanglei, Dai Kesheng, Yuan Yanhong, Zhang Weilin, Yan Rong, and Zhao Lili

Subjects
Immunology, Cell Biology, Hematology, Biology, Filamin, Biochemistry, chemistry.chemical_compound, chemistry, Glycoprotein Ib, Phosphoserine, biology.protein, Phosphorylation, Binding site, Protein kinase A, Binding domain, Proto-oncogene tyrosine-protein kinase Src
Abstract

Conformational changes in von Willebrand factor (VWF) exposed at the injured vessel wall initiate glycoprotein (GP) Ib-IX-dependent platelet adhesion, and simultaneously trigger signaling cascades leading to integrin αIIbβIII activation, platelet spreading, and thrombus formation. The intracellular signaling protein 14-3-3ζ and the membrane skeleton protein filamin A have been confirmed to interact with the cytoplasmic domain of GPIbα and play key roles in regulating the VWF binding function of GPIb-IX. Several phosphoserine containing motifs in GPIb-IX complex, such as Ser609 of GPIbα and Ser166 of GPIbβ, have been confirmed to bind to 14-3-3ζ and involved in the regulation of VWF binding function. We have recently identified a novel 14-3-3ζ binding site located in the filamin A binding domain of GPIbα at Ser559. Phosphorylation of GPIbα at Ser559 not only is important for 14-3-3ζ binding, but also plays a key role in the regulation of VWF binding function of GPIb-IX. However, the protein kinase responsible for Ser559 phosphorylation remains unknown. Here we show that a peptide corresponding to the Arg557-Pro561 region of GPIbα and purified GPIbα could be phosphorylated at Ser559 by the catalytic subunit of protein kinase A (PKA). Ser559 phosphorylation was enhanced by PKA activators and reduced by PKA inhibitors in platelets and Chinese hamster ovary (CHO) cells expressing GPIb-IX. Furthermore, PKA inhibitor enhanced VWF binding to the CHO cells expressing GPIb-IX mutant replacing Ser559 of GPIbα (S559A) with alanine, while reduced in the CHO cells of Ser166 of GPIbβ (S166A) with alanine. GPIb-IX association with filamin A and membrane expression were enhanced in S559A cells, whereas reduced in S166A cells. The peptide disrupting the interaction of 14-3-3ζ with Ser559 of GPIbα inhibited platelet spreading on VWF matrix and GPIb-IX-VWF interaction-induced association of Src with GPIb-IX. These data indicate that Ser559 of GPIbα is phosphorylated by PKA which plays key roles in regulating VWF binding, surface expression, and signaling of GPIb-IX. Disclosures: No relevant conflicts of interest to declare.

Published
2010

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