Vimentin organization modulates the formation of lamellipodia

Brian T. Helfand, Melissa G. Mendez, S. N.Prasanna Murthy, Dale K. Shumaker, Boris Grin, Saleemulla Mahammad, Ueli Aebi, Tatjana Wedig, Yi I. Wu, Klaus M. Hahn, Masaki Inagaki, Harald Herrmann, Robert D. Goldman

Research output: Contribution to journalArticlepeer-review

182 Scopus citations


Vimentin intermediate filaments (VIF) extend throughout the rear and perinuclear regions of migrating fibroblasts, but only nonfilamentous vimentin particles are present in lamellipodial regions. In contrast, VIF networks extend to the entire cell periphery in serum-starved or nonmotile fibroblasts. Upon serum addition or activation of Rac1, VIF are rapidly phosphorylated at Ser-38, a p21-activated kinase phosphorylation site. This phosphorylation of vimentin is coincident with VIF disassembly at and retraction from the cell surface where lamellipodia form. Furthermore, local induction of photoactivatable Rac1 or the microinjection of a vimentin mimetic peptide (2B2) disassemble VIF at sites where lamellipodia subsequently form. When vimentin organization is disrupted by a dominant-negative mutant or by silencing, there is a loss of polarity, as evidenced by the formation of lamellipodia encircling the entire cell, as well as reduced cell motility. These findings demonstrate an antagonistic relationship between VIF and the formation of lamellipodia.

Original languageEnglish (US)
Pages (from-to)1274-1289
Number of pages16
JournalMolecular biology of the cell
Issue number8
StatePublished - Apr 15 2011

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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