AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells

Andrea Dorfleutner, Christian Stehlik, Jing Zhang, Gary E. Gallick, Daniel C. Flynn*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

43 Scopus citations


Regulation of actin organization and dynamics is a highly complex process that involves a number of actin-binding proteins, including capping, branching, severing, sequestering, and cross-linking proteins. The actin-binding and cross-linking protein AFAP-110 is expressed in normal myoepithelial cells. Screening of different breast epithelial cell lines revealed high expression levels of AFAP-110 in the human breast cancer cell lines MDA-MB-231 and MDA-MB-435. Knockdown of AFAP-110 expression in MDA-MB-231 cells does not result in any changes in cell proliferation but did result in a loss of actin stress fiber cross-linking and decreased adhesion to fibronectin. An inducible knockdown approach confirms that MDA-MB-231 breast cancer cells require AFAP-110 expression for stress fiber formation and adhesion. Thus, AFAP-110 may provide cytoskeletal tension through stress fiber formation, which is required for focal adhesion formation. Indeed, we could not detect any focal contacts or focal adhesions in AFAP-110 knockdown cells after adhesion to fibronectin. Although expression levels of crucial focal adhesion components were not influenced by AFAP-110 expression levels, treatment of AFAP-110 knockdown cells with LPA did not result in induction of actin stress fibers and focal adhesions. In summary, AFAP-110 plays an important role in MDA-MB-231 breast cancer cell adhesion possibly by regulating stress filament cross-linking which would promote focal adhesion formation.

Original languageEnglish (US)
Pages (from-to)740-749
Number of pages10
JournalJournal of Cellular Physiology
Issue number3
StatePublished - Dec 2007

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology


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