Metastasis-associated protein S100A4: Spotlight on its role in cell migration

S. Tarabykina, T. R.L. Griffiths, E. Tulchinsky, J. K. Mellon, I. B. Bronstein, M. Kriajevska

Research output: Contribution to journalReview articlepeer-review

94 Citations (Scopus)


S100A4 (also known as Mts1, metastasin, p9Ka, pEL98, CAPL, calvasculin, Fsp-1, placental calcium-binding protein) belongs to the family of EF-hand calcium-binding proteins, whose expression is elevated in a number of pathological conditions. Although it is well documented that S100A4 is expressed in cancer cells and contributes to tumor cell motility and metastatic progression, the exact underlying mechanisms remain elusive. An important characteristic feature of S100 proteins is their dual function, inside and outside the cell. In this review, we focus on the intracellular function of S100A4. The review contains structural analysis of S1004 in comparison with other members of S100 proteins. Possible modes of the interaction of S100 proteins with targets are described. Several examples of best-studied molecular interactions involving S100A4 with heavy chain of nonmuscle myosin IIA, LAR-interacting protein liprin β1 and tumor suppressor protein p53 are provided. We suggest that the binding of S100A4 to these molecules is critical for the S100A4 function. Further studies of the implications of these interactions in different molecular pathways may shed additional light on the role of S100A4 protein in the control of tumor cell motility and migration. We discuss the approaches for down-regulation of S100A4 expression and their potential for application in the clinics.

Original languageEnglish
Pages (from-to)217-228
Number of pages12
JournalCurrent Cancer Drug Targets
Issue number3
Publication statusPublished - May 1 2007
Externally publishedYes


  • Calcium-binding protein
  • EF-hand
  • Liprin beta1
  • Migration
  • Nonmuscle myosin IIA
  • p53
  • S100A4

ASJC Scopus subject areas

  • Oncology
  • Pharmacology
  • Drug Discovery
  • Cancer Research


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