Biology of the Cell

Cover image for Vol. 109 Issue 7

Early View (Online Version of Record published before inclusion in an issue)

Edited By: René-Marc Mège, Paris, France

Impact Factor: 2.649

ISI Journal Citation Reports © Ranking: 2016: 118/189 (Cell Biology)

Online ISSN: 1768-322X


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  1. Research articles

    1. You have full text access to this OnlineOpen article
      Mechanotransduction properties of the cytoplasmic tail of PECAM-1

      Jessica L. Snyder, Elena McBeath, Tamlyn N. Thomas, Yi Jen Chiu, Robert L. Clark and Keigi Fujiwara

      Version of Record online: 13 JUL 2017 | DOI: 10.1111/boc.201600079

      Thumbnail image of graphical abstract

      Research article: We proposed earlier that PECAM-1 is an endothelial cell mechanotransducer and that externally applied forces stretch the PECAM-1 cytoplasmic tail (PECAM-1cyt), exposing a hidden tyrosine which allows it to be phosphorylated by Fyn. If so, PECAM-1cyt could have some folded structure that can be mechanically unravelled. In this study, we show force spectroscopic data on PECAM-1cyt supporting our idea. The figure shows mechanoactivation of PECAM-1, which induces mechanosignalling through proteins such as ERK1/2, a known shear stress-activated MAP kinase.


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