Elongation factor 1α is a component of the subcortical actin bundles of characean algae.

Collings, David A.; Wasteneys, Geoffrey O.; Miyazaki, Motoichi; Williamson, R. E.

doi:10.1006/cbir.1994.1025

Cited by 36 publications

(26 citation statements)

References 21 publications

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“…Consistent with a predicted role of eEF-1A in regulating cytoskeletal structure, in situ studies have shown that eEF-1A is associated with both F-actin (Dharmawardhane et al, 1991;Collings et al, 1994;Clore et al, 1996;Sun et al, 1997) and tubulin (Durso and Cyr, 1994;Durso et al, 1996). Importantly, the distribution of eEF-1A changes when Dictyostelium discoideum.…”

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confidence: 63%

Phosphoglycerylethanolamine Posttranslational Modification of Plant Eukaryotic Elongation Factor 1α1

et al. 1998

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confidence: 63%

Phosphoglycerylethanolamine Posttranslational Modification of Plant Eukaryotic Elongation Factor 1α1

et al. 1998

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“…In plants, actin filament bundles could be gen- erated in a comparable way. Villins might work coordinately with fimbrins (Kovar et al, 2000), formins (Cheung and Wu, 2004;Favery et al, 2004;Michelot et al, 2005;Ye et al, 2009), LIM proteins (Thomas et al, 2006(Thomas et al, , 2007, and/or elongation factor 1a (Collings et al, 1994) in the formation of thick actin filament bundles. Consistent with this idea, fimbrin has been proposed to cross-link actin filament bundles generated by other actin-bundling proteins, such as villin (Matova et al, 1999;Wu et al, 2010).…”

Section: Vln2 and Vln3 Play A Role In Actin Filament Organization In mentioning

confidence: 99%

“…There are four known families of actin-bundling proteins in plants: villins (Vidali et al, 1998;Klahre et al, 2000;Tominaga et al, 2000;Yokota et al, 2003;Huang et al, 2005;Yokota et al, 2005;Khurana et al, 2010;Zhang et al, 2010), fimbrins (Kovar et al, 2000(Kovar et al, , 2001, formins (Cheung and Wu, 2004;Favery et al, 2004;Michelot et al, 2005;Ye et al, 2009), and LIM proteins (Thomas et al, 2006(Thomas et al, , 2008Wang et al, 2008;Papuga et al, 2010). In addition, elongation factor 1a (Collings et al, 1994;Gungabissoon et al, 2001) has been shown to have actin filament-bundling properties as well. The presence of these different actin-bundling proteins suggests that their combined actions can result in several types of actin filament bundles, which differ in form and function (Thomas et al, 2009).…”

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confidence: 99%

Arabidopsis VILLIN2 and VILLIN3 Are Required for the Generation of Thick Actin Filament Bundles and for Directional Organ Growth

Honing

Kieft²,

Emons³

et al. 2011

Plant Physiology

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In plant cells, actin filament bundles serve as tracks for myosin-dependent organelle movement and play a role in the organization of the cytoplasm. Although virtually all plant cells contain actin filament bundles, the role of the different actinbundling proteins remains largely unknown. In this study, we investigated the role of the actin-bundling protein villin in Arabidopsis (Arabidopsis thaliana). We used Arabidopsis T-DNA insertion lines to generate a double mutant in which VILLIN2 (VLN2) and VLN3 transcripts are truncated. Leaves, stems, siliques, and roots of vln2 vln3 double mutant plants are twisted, which is caused by local differences in cell length. Microscopy analysis of the actin cytoskeleton showed that in these double mutant plants, thin actin filament bundles are more abundant while thick actin filament bundles are virtually absent. In contrast to full-length VLN3, truncated VLN3 lacking the headpiece region does not rescue the phenotype of the vln2 vln3 double mutant. Our results show that villin is involved in the generation of thick actin filament bundles in several cell types and suggest that these bundles are involved in the regulation of coordinated cell expansion.The plant actin cytoskeleton plays an essential role in cell division, cytoplasmic organization, cytoplasmic streaming, cell growth, and, consequently, plant morphogenesis. Actin-binding proteins modulate the formation and dynamics of F-actin and its configuration. Among these proteins are the actin-bundling proteins, which are able to cross-link adjacent actin filaments, resulting in bundles consisting of several parallel actin filaments (Thomas et al., 2009). In plant cells, bundling of actin filaments occurs (Thomas et al., 2009), which is likely mediated by actin-bundling proteins. There are four known families of actin-bundling proteins in plants: villins (Vidali et al

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“…3C). eEF1A is present mainly in the cytoplasm of cells (34), but a small population of eEF1A has been identified previously in the nucleus (35)(36)(37)(38). These two populations of eEF1A may play different physiological roles.…”

Section: Fig 6 Mutation On Sermentioning

confidence: 99%

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

Piazzi

Bavelloni

Faenza

et al. 2010

Molecular & Cellular Proteomics

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Recent data indicate that some PKC isoforms are translocated to the nucleus, in response to certain stimuli, where they play an important role in nuclear signaling events. To identify novel interacting proteins of conventional PKC (cPKC) at the nuclear level during myogenesis and to find new PKC isozyme-specific phosphosubstrates, we performed a proteomics analysis of immunoprecipitated nuclear samples from mouse myoblast C2C12 cells following insulin administration. Using a phospho(Ser)-PKC substrate antibody, specific interacting proteins were identified by LC-MS/MS spectrometry. A total of 16 proteins with the exact and complete motif recognized by the phospho-cPKC substrate antibody were identified; among these, particular interest was given to eukaryotic elongation factor 1␣ (eEF1A). Nuclear eEF1A was focalized in the nucleoli, and its expression was observed to increase following insulin treatment. Of the cPKC isoforms, only PKC␤I was demonstrated to be expressed in the nucleus of C2C12 myocytes and to coimmunoprecipitate with eEF1A. In-depth analysis using site-directed mutagenesis revealed that PKC␤I could phosphorylate Ser 53 of the eEF1A2 isoform and that the association between eEF1A2 and PKC␤I was dependent on the phosphorylation status of eEF1A2. Molecular & Cellular Proteomics 9:2719 -2728, 2010.

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Elongation factor 1α is a component of the subcortical actin bundles of characean algae.

Cited by 36 publications

References 21 publications

Phosphoglycerylethanolamine Posttranslational Modification of Plant Eukaryotic Elongation Factor 1α1

Phosphoglycerylethanolamine Posttranslational Modification of Plant Eukaryotic Elongation Factor 1α1

Arabidopsis VILLIN2 and VILLIN3 Are Required for the Generation of Thick Actin Filament Bundles and for Directional Organ Growth

eEF1A Phosphorylation in the Nucleus of Insulin-stimulated C2C12 Myoblasts

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