Intermediate Filaments: Molecular Structure, Assembly Mechanism, and Integration Into Functionally Distinct Intracellular Scaffolds

DOI Web Site 被引用文献11件
  • Harald Herrmann
    Department of Cell Biology, German Cancer Research Center, D-69120 Heidelberg, Germany;
  • Ueli Aebi
    Department of Cell Biology, German Cancer Research Center, D-69120 Heidelberg, Germany;

書誌事項

公開日
2004-06
DOI
  • 10.1146/annurev.biochem.73.011303.073823
公開者
Annual Reviews

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<jats:p>▪ Abstract  The superfamily of intermediate filament (IF) proteins contains at least 65 distinct proteins in man, which all assemble into ∼10 nm wide filaments and are principal structural elements both in the nucleus and the cytoplasm with essential scaffolding functions in metazoan cells. At present, we have only circumstantial evidence of how the highly divergent primary sequences of IF proteins lead to the formation of seemingly similar polymers and how this correlates with their function in individual cells and tissues. Point mutations in IF proteins, particularly in lamins, have been demonstrated to lead to severe, inheritable multi-systemic diseases, thus underlining their importance at several functional levels. Recent structural work has now begun to shed some light onto the complex fine tuning of structure and function in these fibrous, coiled coil forming multidomain proteins and their contribution to cellular physiology and gene regulation.</jats:p>

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