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Nat Rev Mol Cell Biol. 2014 Mar;15(3):163-77. doi: 10.1038/nrm3753.

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

Author information

1
Departments of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
2
1] Departments of Molecular and Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. [2] Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA. [3] Veterans Affairs Ann Arbor Healthcare System, Ann Arbor, Michigan 48109, USA.

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.

PMID:
24556839
PMCID:
PMC4079540
DOI:
10.1038/nrm3753
[Indexed for MEDLINE]
Free PMC Article

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