Literature DB >> 24556839

Post-translational modifications of intermediate filament proteins: mechanisms and functions.

Natasha T Snider1, M Bishr Omary2.   

Abstract

Intermediate filaments (IFs) are cytoskeletal and nucleoskeletal structures that provide mechanical and stress-coping resilience to cells, contribute to subcellular and tissue-specific biological functions, and facilitate intracellular communication. IFs, including nuclear lamins and those in the cytoplasm (keratins, vimentin, desmin, neurofilaments and glial fibrillary acidic protein, among others), are functionally regulated by post-translational modifications (PTMs). Proteomic advances highlight the enormous complexity and regulatory potential of IF protein PTMs, which include phosphorylation, glycosylation, sumoylation, acetylation and prenylation, with novel modifications becoming increasingly appreciated. Future studies will need to characterize their on-off mechanisms, crosstalk and utility as biomarkers and targets for diseases involving the IF cytoskeleton.

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Year:  2014        PMID: 24556839      PMCID: PMC4079540          DOI: 10.1038/nrm3753

Source DB:  PubMed          Journal:  Nat Rev Mol Cell Biol        ISSN: 1471-0072            Impact factor:   94.444


  169 in total

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Review 4.  Posttranslational modifications of desmin and their implication in biological processes and pathologies.

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  172 in total

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3.  Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.

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Journal:  RSC Adv       Date:  2015-01-01       Impact factor: 3.361

Review 6.  Multifaceted role of keratins in epithelial cell differentiation and transformation.

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10.  Mutation of caspase-digestion sites in keratin 18 interferes with filament reorganization, and predisposes to hepatocyte necrosis and loss of membrane integrity.

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