2010
DOI: 10.1091/mbc.e09-09-0829
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Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins

Abstract: Actin arginylation regulates lamella formation in motile fibroblasts, but the underlying molecular mechanisms are unknown. Here, we found that actin regulation by arginylation affects its biochemical properties and binding of actin-associated proteins, modulating the overall structural organization of actin filaments in the cell.

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Cited by 91 publications
(87 citation statements)
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“…A significant proportion of β-actin protein at the leading lamella prior to cell-cell contact and adherens junction assembly is posttranslationally arginylated, preventing tight packing and consequently favoring branched filament polymerization (Karakozova et al 2006). In contrast, linear actin filaments, required to stabilize and anchor adherens junction complexes, are assembled from nonarginylated β-actin monomers (Saha et al 2010). Consequently, we hypothesize that the monomer required for linear actin filament polymerization at cell contact sites during adherens junction assembly are products of locally translated β-actin.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…A significant proportion of β-actin protein at the leading lamella prior to cell-cell contact and adherens junction assembly is posttranslationally arginylated, preventing tight packing and consequently favoring branched filament polymerization (Karakozova et al 2006). In contrast, linear actin filaments, required to stabilize and anchor adherens junction complexes, are assembled from nonarginylated β-actin monomers (Saha et al 2010). Consequently, we hypothesize that the monomer required for linear actin filament polymerization at cell contact sites during adherens junction assembly are products of locally translated β-actin.…”
Section: Discussionmentioning
confidence: 99%
“…For example, E-cadherin directly regulates actin filament polymerization during the contact initiation stage of epithelial adherens junction assembly by binding and localizing Arp2/3 complexes to cellcell contact sites (Kovacs et al 2002b). Also during the contact initiation stage of adherens junction assembly, post-translationally arginylated-β-actin monomers polymerize into branched filament arrays driving lamellar protrusion in areas with high concentrations of activated Arp2/3 complexes (Kovacs et al 2002a;Karakozova et al 2006;Saha et al 2010). Thereafter, E-cadherin homophilic interactions stimulate accumulation of other actin-binding proteins including formin, mDia, and Ena/Vasp to the contact zone, where they stimulate linear filament polymerization to drive contact expansion (Sahai and Marshall 2002;Kobielak et al 2004; 3 Scott et al 2006;Carramusa et al 2007).…”
Section: Introductionmentioning
confidence: 99%
“…When one then compares this to the reported specificity of the Ubr proteins, it appears that the yeast UBR1 protein exhibits a low specificity for acidic penultimate residues (Choi et al 2010), such that Ate1 products in yeast are suboptimal substrates for UBR1. Further investigations may reveal this apparent dichotomy may be to tune the half-life of protein substrates or may correlate with emerging alternative roles for protein arginylation (Cha-Molstad et al 2015;Cornachione et al 2014;Jiang et al 2016;Saha et al 2010;Zhang et al 2015).…”
Section: Recent Work Bymentioning
confidence: 99%
“…Intriguingly, in many cases the destabilizing effect of arginylation on the corresponding target proteins in mouse was lacking and most arginylated N-terminal amino acids were not classical destabilizing residues in the context of the N-end rule pathway (23). In fact, arginylation of mammalian proteins can increase stability and influence oligomerization (25,26). In contrast, arginylation of glutamic acid residues can also target proteins via p62 (Sequestosome-1) binding to autophagy-mediated degradation in mammalian cell lines (27).…”
mentioning
confidence: 99%