Application of High-Content Analysis to the Study of Post-Translational Modifications of the Cytoskeleton

Drake, Peter J. M.; Griffiths, Gareth; Shaw, Leila; Benson, Rod P.; Corfe, Bernard M.

doi:10.1021/pr8006396

Cited by 27 publications

(34 citation statements)

References 24 publications

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“…One example is vimentin, which is acetylated on several lysine residues [5], another is cytokeratin 8, which is acetylated on three lysine residues. In contrast to tubulin and actin however, in this case, acetylation seems to destabilize the polymer [120, 121]. …”

Section: Functional Implications Of Cytoplasmic Lysine Acetylationmentioning

confidence: 99%

The Tale of Protein Lysine Acetylation in the Cytoplasm

Sadoul

Wang

Diagouraga

et al. 2010

BioMed Research International

131

130

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Reversible posttranslational modification of internal lysines in many cellular or viral proteins is now emerging as part of critical signalling processes controlling a variety of cellular functions beyond chromatin and transcription. This paper aims at demonstrating the role of lysine acetylation in the cytoplasm driving and coordinating key events such as cytoskeleton dynamics, intracellular trafficking, vesicle fusion, metabolism, and stress response.

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Section: Functional Implications Of Cytoplasmic Lysine Acetylationmentioning

confidence: 99%

The Tale of Protein Lysine Acetylation in the Cytoplasm

Sadoul

Wang

Diagouraga

et al. 2010

BioMed Research International

131

130

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“…Although the role of these acetylations remains unclear, acetylation is recognized as an important PTM of proteins that regulates protein function. In contrast with tubulin and actin, however, acetylation has been shown to destabilize the polymer [22,23]. For example, the increase of acetylation was coupled with a breakdown in intermediate filaments in the cytoskeleton [22].…”

Section: Biological Significance Of Lysine Acetylation Of Cytoskeletamentioning

confidence: 99%

Lysine post-translational modifications and the cytoskeleton

Zencheck

Xiao

Weiss

2012

Essays in Biochemistry

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PTMs (post-translational modifications) of lysine residues have proven to be major regulators of gene expression, protein–protein interactions, and protein processing and degradation. This is of particular importance in regulating the cytoskeleton, an enormously complex system of proteins responsible for cell motility, intracellular trafficking, and maintenance of cell form and structure. The cytoskeleton is present in all cells, including eukaryotes and prokaryotes, and comprises structures such as flagella, cilia and lamellipodia which play critical roles in intracellular transport and cellular division. Cytoskeletal regulation relies on numerous multi-component assemblies. In this chapter, we focus on the regulation of the cytoskeleton by means of PTMs of lysine residues on the cytoskeletal subunits and their accessory proteins. We specifically address the three main classes of cytoskeletal proteins in eukaryotes that polymerize into filaments, including microfilaments (actin filaments), intermediate filaments and microtubules. We discuss the identification and biological importance of lysine acetylation, a regulator of all three filament types. We also review additional lysine modifications, such as ubiquitination and SUMOylation, and their role in protein regulation and processing.

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“…Numerous studies have pointed to keratins 8 and 18 as two of the pivotal intermediate filaments involved in cellular homeostasis and the absence of these proteins may sensitise epithelial cells, including colorectal cancer cells, to Fas and TNF‐α‐mediated apoptosis 13, 14. In particular, the function and stability of keratin 8 in vitro is believed to be dependent on its post‐translational modification where there is evidence to indicate that butyrate increases keratin 8 acetylation and that this has a potentially negative effect on cytoskeletal integrity 15, 16. Furthermore, keratins 8, 18 and 19 are believed to be cleaved by caspases during the apoptotic process 17.…”

Section: Resultsmentioning

confidence: 99%

A combined free‐flow electrophoresis and DIGE approach to identify proteins regulated by butyrate in HT29 cells

et al. 2011

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Many biologically active agents exert a pleiotropic response in cells and tissues. This presents challenges in descriptive and comparative analysis of the proteome in response to these agents. Although free-flow electrophoresis has been applied in a number of proteomic studies as a protein separation technique, the combination of free-flow electrophoresis and DIGE has not yet been investigated for comparative proteomic analysis. In this study, we have compared the effects of butyrate on HT29 colorectal cancer cells with a particular focus on apoptosis and describe the utility of a novel approach combining free-flow electrophoresis with DIGE to identify differentially expressed proteins. We verify the results obtained by the combined free-flow electrophoresis and DIGE approach with Western blot analysis of selected proteins. We also report for the first time the regulation of a number of proteins by butyrate in HT29 colorectal cells including peptidyl-prolyl cis-trans isomerase A (cyclophilin A) and profilin-1.

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Application of High-Content Analysis to the Study of Post-Translational Modifications of the Cytoskeleton

Cited by 27 publications

References 24 publications

The Tale of Protein Lysine Acetylation in the Cytoplasm

The Tale of Protein Lysine Acetylation in the Cytoplasm

Lysine post-translational modifications and the cytoskeleton

A combined free‐flow electrophoresis and DIGE approach to identify proteins regulated by butyrate in HT29 cells

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