The phytotoxin fusicoccin promotes platelet aggregation via 14-3-3–glycoprotein Ib-IX-V interaction1

The phytotoxin fusicoccin promotes platelet aggregation via 14-3-3-glycoprotein Ib-IX-V interaction.

The fungal toxin fusicoccin induces plant wilting by affecting ion transport across the plasma membrane of plant cell. The activity of this toxin is so far unknown in humans. In the present study we show that fusicoccin is able to affect the platelet aggregation process. The toxin associates with platelet intracellular binding sites and induces aggregation in platelet-rich plasma in a dose-depe...

A functional 14-3-3 –independent association of PI3-kinase with glycoprotein Ib , the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex

1Department of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; 2Puget Sound Blood Center and Division of Hematology, University of Washington, Seattle; 3Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Australia; and 4Department of Human Immunology, Institute of Medical and Ve...

Platelet Glycoprotein Ib-IX and Malignancy

Alpha-granule membrane mirrors the platelet plasma membrane and contains the glycoproteins Ib, IX, and V.

We have recently shown that several components from the platelet plasma membrane were also present at different rates in the alpha-granule membrane. This is the case for the glycoprotein (GP) IIb-IIIa (CD41), CD36, CD9, PECAM1, and Rap1b, while the GPIB-IX-V complex was considered to escape the rule. In this investigation, we studied the subcellular localization of GPIb, GPIX, and GPV in the re...

Interaction of calmodulin with the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex.

Engagement of platelet membrane glycoprotein (GP) Ib-IX-V by von Willebrand factor triggers Ca(++)-dependent activation of alphaIIbbeta3, resulting in (patho)physiological thrombus formation. It is demonstrated here that the cytoplasmic domain of GPIb-IX-V associates with cytosolic calmodulin. First, an anti-GPIbalpha antibody coimmunoprecipitated GPIb-IX and calmodulin from platelet lysates. F...