Actin bundling and polymerisation properties of eukaryotic elongation factor 1 alpha (eEF1A), histone H2A–H2B and lysozyme in vitro

2011 ◽  
Vol 176 (3) ◽  
pp. 370-378 ◽  
Author(s):  
Annette Doyle ◽  
Steven R. Crosby ◽  
David R. Burton ◽  
Francis Lilley ◽  
Mark F. Murphy
2008 ◽  
Vol 28 (14) ◽  
pp. 4549-4561 ◽  
Author(s):  
Sujeeve Jeganathan ◽  
Anne Morrow ◽  
Anahita Amiri ◽  
Jonathan M. Lee

ABSTRACT Eukaryotic elongation factor 1 alpha 2 (eEF1A2) is a transforming gene product that is highly expressed in human tumors of the ovary, lung, and breast. eEF1A2 also stimulates actin remodeling, and the expression of this factor is sufficient to induce the formation of filopodia, long cellular processes composed of bundles of parallel actin filaments. Here, we find that eEF1A2 stimulates formation of filopodia by increasing the cellular abundance of cytosolic and plasma membrane-bound phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2]. We have previously reported that the eEF1A2 protein binds and activates phosphatidylinositol-4 kinase III beta (PI4KIIIβ), and we find that production of eEF1A2-dependent PI(4,5)P2 and generation of filopodia require PI4KIIIβ. Furthermore, PI4KIIIβ is itself capable of activating both the production of PI(4,5)P2 and the creation of filopodia. We propose a model for extrusion of filopodia in which eEF1A2 activates PI4KIIIβ, and activated PI4KIIIβ stimulates production of PI(4,5)P2 and filopodia by increasing PI4P abundance. Our work suggests an important role for both eEF1A2 and PI4KIIIβ in the control of PI(4,5)P2 signaling and actin remodeling.


Pathogens ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 702
Author(s):  
Hang Zhou ◽  
Yue Guan ◽  
Meng Feng ◽  
Yongfeng Fu ◽  
Hiroshi Tachibana ◽  
...  

Entamoeba histolytica is the causative agent of amoebiasis. This disease results in 40,000 to 100,000 deaths annually. The pathogenic molecules involved in the invasion of trophozoites had been constantly being clarified. This study explored the role of elongation factor 1 alpha (EF1a) in E. histolytica pathogenicity. Biolayer interferometry binding and pull-down assays suggest that EF1a and intermediate subunit of lectin (Igl) binding are specific. Submembranous distribution of EF1a closely aligns with the localization of Igl, which appear in abundance on membranes of trophozoites. Messenger RNA (mRNA) expression of EF1a is positively correlated with trends in Igl levels after co-incubation with Chinese hamster ovary (CHO) cells in vitro, suggesting a regulatory linkage between these proteins. Erythrophagocytosis assays also imply a role for EF1a in phagocytosis. Finally, EF1a and actin are collocated in trophozoites. These results indicated elongation factor 1a is associated with E. histolytica phagocytosis, and the relationships between EF1a, Igl, and actin are worth further study to better understand the pathogenic process.


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