The actomyosin network and cellular motility: a S100A4 regulatory view into the process

Research output: Chapter in Book/Published conference outputChapter (peer-reviewed)peer-review


Cell migration is a fundamental process responsible for numerous physiological and physiopathological conditions such as inflammation, embryogenesis and cancer. This central aspect of cell biology has seen quantum leaps in our understanding of the coordinated regulations, both spatial and temporal of numerous cytoskeletal proteins and their orchestrations. At the molecular level, this dynamic cellular process can be naively summarised as an engineered cycle composed of three distinct phases of (1) formation of cellular protrusion to initiate contact followed by (2) the adhesion with the external environment/cell-extracellular established connection and (3) the actomyosin force generation to consequently remodel the cytoskeleton. A prominent factor that regulates cellular motility is S100A4, a protein that has received constant attention for its significant role in cellular migration. Consequently, and in order to focus further the impact of this work, the present chapter aims to review some of the actomyosin proteins/complexes that have been demonstrated to be crucial players of the cyclic migration process but are also S100A4 interactors. In doing so, this chapter aims to capture a picture of how expression of this small, calcium-binding protein may, in essence, remodel at different levels the actin organisation and fulfil the motility engineered cycle of protrusion, attachments and contractions.
Original languageEnglish
Title of host publicationCytoskeleton - structure, dynamics, function and disease
EditorsJose C. Jimenez-Lopez
Number of pages37
ISBN (Electronic)978-953-51-3170-0
ISBN (Print)978-953-51-3169-4
Publication statusPublished - 17 May 2017

Bibliographical note

© 2017 The Author(s). Licensee lnTech. This chapter is distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


  • S100A4
  • actin
  • Arp2/3
  • formin
  • tropomyosin
  • myosin
  • Rho-GTPAses
  • Rhotekin


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