Vimentin organization modulates the formation of lamellipodia |
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Authors: | Helfand Brian T Mendez Melissa G Murthy S N Prasanna Shumaker Dale K Grin Boris Mahammad Saleemulla Aebi Ueli Wedig Tatjana Wu Yi I Hahn Klaus M Inagaki Masaki Herrmann Harald Goldman Robert D |
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Institution: | Department of Urology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. |
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Abstract: | 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. |
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