Intermediate filaments: primary determinants of cell architecture and plasticity
Harald Herrmann, Sergei V. Strelkov, Peter Burkhard, Ueli Aebi
Harald Herrmann, Sergei V. Strelkov, Peter Burkhard, Ueli Aebi
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Intermediate filaments: primary determinants of cell architecture and plasticity

Abstract

Intermediate filaments (IFs) are major constituents of the cytoskeleton and nuclear boundary in animal cells. They are of prime importance for the functional organization of structural elements. Depending on the cell type, morphologically similar but biochemically distinct proteins form highly viscoelastic filament networks with multiple nanomechanical functions. Besides their primary role in cell plasticity and their established function as cellular stress absorbers, recently discovered gene defects have elucidated that structural alterations of IFs can affect their involvement both in signaling and in controlling gene regulatory networks. Here, we highlight the basic structural and functional properties of IFs and derive a concept of how mutations may affect cellular architecture and thereby tissue construction and physiology.

Authors

Harald Herrmann, Sergei V. Strelkov, Peter Burkhard, Ueli Aebi

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Figure 5

Impact of a point mutation in vimentin coil 1A on filament elongation both in vitro and in vivo.

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Impact of a point mutation in vimentin coil 1A on filament elongation bo...
(A) Hypothetical model depicting that coil 1A may have a tendency to open up with the authentic tyrosine 117, shown in extreme conformation. (B) Side stereo view of the atomic structure of coil 1A from the vimentin mutant Y117L, exhibiting a bona fide coiled coil. Residues bounded by the first and the last knobs-into-hole interaction are colored in cyan. Residues at a positions are shown in yellow and those at d positions are shown in magenta. The N terminus is marked N, and the C terminus is marked C. The residue types and numbers of the core positions are indicated. (C) Transfection of mouse embryonic fibroblasts derived from vimentin-knockout mice (130) with the vimentin mutant Y117L, followed by indirect immunofluorescence microscopy with antibodies specific for human vimentin, revealing dot-like structures exclusively. Note the regular shaped particles that on occasion are lined up, possibly being situated on a fibrillar structure such as a MT (inset). Scale bar: 20 μm. A is reproduced with permission from EMBO journal (43). B and C are reproduced with permission from Journal of molecular biology (92).