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Lamellipodin promotes actin assembly by clustering Ena/VASP proteins and tethering them to actin filaments

Authors :
Scott D Hansen
R Dyche Mullins
Source :
eLife, Vol 4 (2015)
Publication Year :
2015
Publisher :
eLife Sciences Publications Ltd, 2015.

Abstract

Enabled/Vasodilator (Ena/VASP) proteins promote actin filament assembly at multiple locations, including: leading edge membranes, focal adhesions, and the surface of intracellular pathogens. One important Ena/VASP regulator is the mig-10/Lamellipodin/RIAM family of adaptors that promote lamellipod formation in fibroblasts and drive neurite outgrowth and axon guidance in neurons. To better understand how MRL proteins promote actin network formation we studied the interactions between Lamellipodin (Lpd), actin, and VASP, both in vivo and in vitro. We find that Lpd binds directly to actin filaments and that this interaction regulates its subcellular localization and enhances its effect on VASP polymerase activity. We propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their polymerase activity by tethering them to filaments. This interaction represents one more pathway by which growing actin filaments produce positive feedback to control localization and activity of proteins that regulate their assembly.

Details

Language :
English
ISSN :
2050084X
Volume :
4
Database :
Directory of Open Access Journals
Journal :
eLife
Publication Type :
Academic Journal
Accession number :
edsdoj.3d40b4067b55450fa5a682cfa8064f05
Document Type :
article
Full Text :
https://doi.org/10.7554/eLife.06585