2008
DOI: 10.1096/fj.06-7654com
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Profilin induces lamellipodia by growth factor independent mechanism

Abstract: Profilin has been implicated in cell motility and in a variety of cellular processes, such as membrane extension, endocytosis, and formation of focal complexes. In vivo, profilin replenish the pool of ATP-actin monomers by increasing the rate of nucleotide exchange of ADP-actin for ATP-actin, promoting the incorporation of new actin monomers at the barbed end of actin filaments. For this report, we generated a membrane-permeable version of profilin I (PTD4-PfnI) for the alteration of intracellular profilin lev… Show more

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Cited by 16 publications
(28 citation statements)
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“…The results from experiments using membranepermeable profilin-I (PTD4-PfnI) suggest that profilin-I induces lamellipodia formation independently of the presence of EGF in primary bovine trabecular meshwork cells (Syriani et al 2008). The effects are time-and dosagedependent and specific to the profilin-I isoform: the H133S mutation in the poly-L-proline binding domain showed a reduced ability to induce lamellipodia, and the H199E mutation in the actin binding domain failed to induce membrane spreading (Syriani et al 2008).…”
Section: Jankementioning
confidence: 99%
See 1 more Smart Citation
“…The results from experiments using membranepermeable profilin-I (PTD4-PfnI) suggest that profilin-I induces lamellipodia formation independently of the presence of EGF in primary bovine trabecular meshwork cells (Syriani et al 2008). The effects are time-and dosagedependent and specific to the profilin-I isoform: the H133S mutation in the poly-L-proline binding domain showed a reduced ability to induce lamellipodia, and the H199E mutation in the actin binding domain failed to induce membrane spreading (Syriani et al 2008).…”
Section: Jankementioning
confidence: 99%
“…The effects are time-and dosagedependent and specific to the profilin-I isoform: the H133S mutation in the poly-L-proline binding domain showed a reduced ability to induce lamellipodia, and the H199E mutation in the actin binding domain failed to induce membrane spreading (Syriani et al 2008). Profilin-I levels were found to be lower in hepatocarcinoma (SMMC-7721) cells and the all-trans retinoic acid-induced inhibition of proliferation and migration was found to be mediated through profilin-I expression.…”
Section: Jankementioning
confidence: 99%
“…Pfn1 is a ROCK substrate (Shao et al, 2008) known to promote lamellipodia formation in different cell types (Cao et al, 1992;Syriani et al, 2008). Accordingly, we show that in SCs exposed to LPA or in Ilk mutant sciatic nerves in which ROCK activation is increased, Pfn1 is phosphorylated on Ser-137 by ROCK.…”
Section: Pfn1 Regulates Sc Radial Lamellipodia Independently Of Rac1mentioning
confidence: 70%
“…Pfn1 is an actin remodeling protein that is capable of regulating lamellipodia formation in different cell types (Cao et al, 1992;Syriani et al, 2008), and is a ROCK substrate (Shao et al, 2008). Therefore, it is a strong candidate in mediating lamellipodia formation downstream of Rho/ROCK in SCs.…”
Section: Rho/rock Signaling Regulates Radial Lamellipodia Formation Imentioning
confidence: 99%
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