Investigating lasp-2 in cell adhesion: New binding partners and roles in motility

Katherine T. Bliss, Miensheng Chu, Colin M. Jones-Weinert, Carol C. Gregorio

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Focal adhesions are intricate protein complexes that facilitate cell attachment, migration, and cellular communication. Lasp-2 (LIM-nebulette), a member of the nebulin family of actin-binding proteins, is a newly identified component of these complexes. To gain further insights into the functional role of lasp-2, we identified two additional binding partners of lasp-2: the integral focal adhesion proteins vinculin and paxillin. Of interest, the interaction of lasp-2 with its binding partners vinculin and paxillin is significantly reduced in the presence of lasp-1, another nebulin family member. The presence of lasp-2 appears to enhance the interaction of vinculin and paxillin with each other; however, as with the interaction of lasp-2 with vinculin or paxillin, this effect is greatly diminished in the presence of excess lasp-1. This suggests that the interplay between lasp-2 and lasp-1 could be an adhesion regulatory mechanism. Lasp-2's potential role in metastasis is revealed, as overexpression of lasp-2 in either SW620 or PC-3B1 cells-metastatic cancer cell lines-increases cell migration but impedes cell invasion, suggesting that the enhanced interaction of vinculin and paxillin may functionally destabilize focal adhesion composition. Taken together, these data suggest that lasp-2 has an important role in coordinating and regulating the composition and dynamics of focal adhesions.

Original languageEnglish (US)
Pages (from-to)995-1006
Number of pages12
JournalMolecular biology of the cell
Issue number7
StatePublished - Apr 1 2013

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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