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Review
. 2008 Feb;20(1):28-34.
doi: 10.1016/j.ceb.2007.11.003. Epub 2008 Jan 4.

Intermediate filaments: versatile building blocks of cell structure

Robert D Goldman  1 , Boris Grin, Melissa G Mendez, Edward R Kuczmarski
Affiliations
Review

Intermediate filaments: versatile building blocks of cell structure

Robert D Goldman et al. Curr Opin Cell Biol. 2008 Feb.

Abstract

Cytoskeletal intermediate filaments (IF) are organized into a dynamic nanofibrillar complex that extends throughout mammalian cells. This organization is ideally suited to their roles as response elements in the subcellular transduction of mechanical perturbations initiated at cell surfaces. IF also provide a scaffold for other types of signal transduction that together with molecular motors ferries signaling molecules from the cell periphery to the nucleus. Recent insights into their assembly highlight the importance of co-translation of their precursors, the hierarchical organization of their subunits in the formation of unit-length filaments (ULF) and the linkage of ULF into mature apolar IF. Analyses by atomic force microscopy reveal that mature IF are flexible and can be stretched to over 300% of their length without breaking, suggesting that intrafilament subunits can slide past one another when exposed to mechanical stress and strain. IF also play a role in the organization of organelles by modulating their motility and providing anchorage sites within the cytoplasm.

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Figures

Figure 1
Figure 1. Vimentin intermediate filament network
A Chinese hamster ovary (CHO) cell fixed and processed for immunofluorescence using anti-vimentin. The IF surround the nucleus and extend to the cell periphery.
Figure 2
Figure 2. Keratin filament network
Rat kangaroo kidney epithelial cells (PtK2) were fixed and processed for immunofluorescence with anti-keratin. The extensive network of tonofibrils (bundles of IF) ranges throughout the cytoplasm and appears to connect the cell surface with the nucleus where there is a juxtanuclear cage.
Figure 3
Figure 3. IF Assembly
Based on a variety of biochemical, physical chemical, electron microscopic and X-ray diffraction studies, the assembly pathway for intermediate filaments is now understood in reasonable detail. Individual protein chains self-assemble to form a parallel, non-staggered coiled-coil dimer (A), and two of these dimers come together in an antiparallel, manner to form a tetramer (B). In turn, 2 tetramers associate to form octamers, and finally 4 octamers join to form the ULF (unit length filament) (C). Individual ULFs join end-to-end to form short filaments (D), and these then grow into longer filaments by the continued addition of ULFs as well as the end-to-end fusion of existing filaments. (The A12 mode of antiparallel overlap of IF dimers is illustrated; see reference [12].)
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