Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-51157
Elife July 9, 2015; 4
Show Gene links Show Anatomy links

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

Hansen SD , Mullins RD .


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.

PubMed ID: 26295568
PMC ID: PMC4543927
Article link: Elife
Grant support: [+]

Species referenced: Xenopus
Genes referenced: abi1 acta1 aicda enah evl lif lyn pfn1 rho rho.2 tbx2 vasp zyx


Article Images: [+] show captions
References [+] :
Akin, Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. 2008, Pubmed