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TitleStructural analysis of receptors and actin polarity in platelet protrusions.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 37, Year 2021
Publish dateSep 14, 2021
AuthorsSimona Sorrentino / Jose Javier Conesa / Ana Cuervo / Roberto Melero / Bruno Martins / Estrella Fernandez-Gimenez / Federico P de Isidro-Gomez / Jimenez de la Morena / Jan-Dirk Studt / Carlos Oscar S Sorzano / Matthias Eibauer / Jose Maria Carazo / Ohad Medalia /
PubMed AbstractDuring activation the platelet cytoskeleton is reorganized, inducing adhesion to the extracellular matrix and cell spreading. These processes are critical for wound healing and clot formation. ...During activation the platelet cytoskeleton is reorganized, inducing adhesion to the extracellular matrix and cell spreading. These processes are critical for wound healing and clot formation. Initially, this task relies on the formation of strong cellular-extracellular matrix interactions, exposed in subendothelial lesions. Despite the medical relevance of these processes, there is a lack of high-resolution structural information on the platelet cytoskeleton controlling cell spreading and adhesion. Here, we present in situ structural analysis of membrane receptors and the underlying cytoskeleton in platelet protrusions by applying cryoelectron tomography to intact platelets. We utilized three-dimensional averaging procedures to study receptors at the plasma membrane. Analysis of substrate interaction-free receptors yielded one main structural class resolved to 26 Å, resembling the αβ integrin folded conformation. Furthermore, structural analysis of the actin network in pseudopodia indicates a nonuniform polarity of filaments. This organization would allow generation of the contractile forces required for integrin-mediated cell adhesion.
External linksProc Natl Acad Sci U S A / PubMed:34504018 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution26.6 Å
Structure data

EMDB-12285:
Platelet integrin from intact cells
Method: EM (subtomogram averaging) / Resolution: 26.6 Å

Source
  • Homo sapiens (human)

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