Nogo-B mediates HeLa cell adhesion and motility through binding of Fibulin-5.
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.
Zhou
Shumin
S
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, Hubei, PR China.
Xiao
Wei
W
Wan
Qingwen
Q
Yi
Changhua
C
Xiao
Feifei
F
Liu
Yingle
Y
Qi
Yipeng
Y
D002448:Cell Adhesion; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D009185:Myelin Proteins / Q000235:genetics / Q000378:metabolism*; D000070798:Nogo Proteins; D021381:Protein Transport
D016326:Extracellular Matrix Proteins; C492373:FBLN5 protein, human; D009185:Myelin Proteins; D000070798:Nogo Proteins; C000603199:RTN4 protein, human