Platelet actin nodules are podosome-like structures dependent on Wiskott–Aldrich syndrome protein and ARP2/3 complex

Natalie S. Poulter, Alice Y. Pollitt, Amy Davies, Dessislava Malinova, Gerard B. Nash, Mike J. Hannon, Zoe Pikramenou, Joshua Z. Rappoport, John H. Hartwig, Dylan M. Owen, Adrian J. Thrasher, Stephen P. Watson () and Steven G. Thomas ()
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Natalie S. Poulter: Centre for Cardiovascular Sciences, The Medical School, University of Birmingham
Alice Y. Pollitt: Centre for Cardiovascular Sciences, The Medical School, University of Birmingham
Amy Davies: PSIBS doctoral training centre, School of Chemistry, University of Birmingham
Dessislava Malinova: Molecular Immunology Unit, UCL Institute of Child Health
Gerard B. Nash: Centre for Cardiovascular Sciences, The Medical School, University of Birmingham
Mike J. Hannon: PSIBS doctoral training centre, School of Chemistry, University of Birmingham
Zoe Pikramenou: School of Chemistry, University of Birmingham
Joshua Z. Rappoport: The Center for Advanced Microscopy and Nikon Imaging Center, Morton 2-681, Northwestern University Feinberg School of Medicine
John H. Hartwig: Brigham and Women’s Hospital, Harvard Medical School
Dylan M. Owen: New Hunt’s House, King’s College London
Adrian J. Thrasher: Molecular Immunology Unit, UCL Institute of Child Health
Stephen P. Watson: Centre for Cardiovascular Sciences, The Medical School, University of Birmingham
Steven G. Thomas: Centre for Cardiovascular Sciences, The Medical School, University of Birmingham

Nature Communications, 2015, vol. 6, issue 1, 1-15

Abstract: Abstract The actin nodule is a novel F-actin structure present in platelets during early spreading. However, only limited detail is known regarding nodule organization and function. Here we use electron microscopy, SIM and dSTORM super-resolution, and live-cell TIRF microscopy to characterize the structural organization and signalling pathways associated with nodule formation. Nodules are composed of up to four actin-rich structures linked together by actin bundles. They are enriched in the adhesion-related proteins talin and vinculin, have a central core of tyrosine phosphorylated proteins and are depleted of integrins at the plasma membrane. Nodule formation is dependent on Wiskott–Aldrich syndrome protein (WASp) and the ARP2/3 complex. WASp−/− mouse blood displays impaired platelet aggregate formation at arteriolar shear rates. We propose actin nodules are platelet podosome-related structures required for platelet–platelet interaction and their absence contributes to the bleeding diathesis of Wiskott–Aldrich syndrome.

Date: 2015
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DOI: 10.1038/ncomms8254

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