Profilin induces lamellipodia by growth factor-independent mechanism

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Enrique SyrianiMiguel Morales

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 levels taking advantage of the protein transduction technique. We show that profilin I induces lamellipodia formation independently of growth factor presence in primary bovine trabecular meshwork (BTM) cells. The effects are time- and concentration-dependent and specific to the profilin I isoform. Profilin II, the neuronal isoform, failed to extend lamellipodia in the same degree as profilin I. H133S, a mutation in the polyproline binding domain, showed a reduced ability to induce lamellipodia. H199E, mutation in the actin binding domain failed to induce membrane spreading and inhibit fetal bovine serum (FBS) -induced lamellipodia extension. Incubation with a synthetic polyproline domain peptide (GP5)3, fused to a transductio...Continue Reading

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Citations

Apr 13, 2012·PloS One·Manik GoelSanjoy K Bhattacharya
Nov 13, 2013·Current Eye Research·Vu T TranSanjoy K Bhattacharya
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May 8, 2021·Journal of Cell Science·Abigail AllenPartha Roy

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