Nogo-B mediates HeLa cell adhesion and motility through binding of Fibulin-5

Biochem Biophys Res Commun. 2010 Jul 23;398(2):247-53. doi: 10.1016/j.bbrc.2010.06.068. Epub 2010 Jun 19.


Nogo-B is a known regulator of neural functions and plays an important role in cell adhesion and migration. To our knowledge, the molecular mechanism behind its regulation of cell motility is still unknown. Here, we identified Fibulin-5, a secreted extracellular matrix protein, as a binding partner of Nogo-B. Using HeLa cells as a model, we found that Nogo-B and Fibulin-5 co-localize in the cytoplasm and plasma membrane. Furthermore, in HeLa cells that overexpress Nogo-B, cell migration and invasion was promoted by the elevated secretion of Fibulin-5. Thus, identification of the Nogo-B binding protein Fibulin-5 may contribute to uncover the pathway in which Nogo-B regulates tumor cell movement.

MeSH terms

  • Cell Adhesion
  • Cell Nucleus / metabolism
  • Cytoplasm / metabolism
  • Endoplasmic Reticulum / metabolism
  • Extracellular Matrix Proteins / genetics
  • Extracellular Matrix Proteins / metabolism*
  • HeLa Cells
  • Humans
  • Myelin Proteins / genetics
  • Myelin Proteins / metabolism*
  • Nogo Proteins
  • Protein Transport


  • Extracellular Matrix Proteins
  • FBLN5 protein, human
  • Myelin Proteins
  • Nogo Proteins
  • RTN4 protein, human