FEBS Letters
Volume 584, Issue 3 , Pages 493-499, 5 February 2010

Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to the plasma membrane and regulates cell elasticity

Edited by Berend Wieringa

  • Balaji Olety

      Affiliations

    • Institute of General Zoology and Genetics, Westfalian Wilhelms-University Münster, Germany
    • ,
  • Mike Wälte

      Affiliations

    • Institute of Physiology II, Westfalian Wilhelms-University Münster, Germany
    • ,
  • Ulrike Honnert

      Affiliations

    • Institute of General Zoology and Genetics, Westfalian Wilhelms-University Münster, Germany
    • ,
  • Hermann Schillers

      Affiliations

    • Institute of Physiology II, Westfalian Wilhelms-University Münster, Germany
    • ,
  • Martin Bähler

      Affiliations

    • Institute of General Zoology and Genetics, Westfalian Wilhelms-University Münster, Germany
    • Corresponding Author InformationCorresponding author. Address: Institut für Allgemeine Zoologie und Genetik, Westfälische Wilhelms Universität, Schlossplatz 5, 48149 Münster, Germany. Fax: +49 251 83 24723.

Received 3 September 2009; received in revised form 10 November 2009; accepted 30 November 2009. published online 07 December 2009.

Abstract 

Immune cells navigate through different environments where they experience different mechanical forces. Responses to external forces are determined by the mechanical properties of a cell and they depend to a large extent on the actin-rich cell cortex. We report here that Myo1G, a previously uncharacterised member of class I myosins, is expressed specifically in haematopoietic tissues and cells. It is associated with the plasma membrane. This association is dependent on a conserved PH-domain-like myosin I tail homology motif and the head domain. However, the head domain does not need to be a functional motor. Knockdown of Myo1G in Jurkat cells decreased cell elasticity significantly. We propose that Myo1G regulates cell elasticity by deformations of the actin network at the cell cortex.

Structured summary

MINT-7307273: MYO1G (uniprotkb:B0I1T2) and Actin (uniprotkb:P60709) colocalize (MI:0403) by fluorescence microscopy (MI:0416) MINT-7307283: TfR (uniprotkb:P02786) and MYO1G (uniprotkb:B0I1T2) colocalize (MI:0403) by cosedimentation through density gradients (MI:0029)

Keywords: Myo1G, Myosin, Actin, Cell elasticity, Haematopoietic, PH-domain

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PII: S0014-5793(09)01039-4

doi:10.1016/j.febslet.2009.11.096

FEBS Letters
Volume 584, Issue 3 , Pages 493-499, 5 February 2010

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