Cytoplasmic linker proteins

Komarova YA, Akhmanova AS, Kojima S, Galjart N, Borisy GG. Cytoplasmic linker proteins promote microtubule rescue in vivo. J. Cell Biol. 2002 159 589-599. 

Although various primary proteins form a variety of intermediate filaments, aU intermediate filaments have a similar structural design. The basic building block, a monomer of IF protein, is a long central a-helix, called rod domain, interrupted by linkers and flanked by an N-terminal head and a C-terminal tail domain as shown in Fig. 3a [49, 55, 56]. Two monomers twist around each other to form a coUed-coil dimer, which is stabilized by a hydrophobic left-handed stripe that winds around the axis of each a-helrx [57], This rod-Uke domain controls the mechanical property of the single intermediate filament. Despite these similarities, there are distinct differences at the tail domain between nuclear IF proteins (e.g., lamin) and cytoplasmic IF proteins (e.g., vimentin) [58]. 

Stress fibers are parallel bundles of actin filaments that develop in the cytoplasm of fibroblasts from the cortical actin network in response to mechanical tension. These often bind to the plasma membrane at focal contacts and, through transmembrane linker glycoproteins, to the extracellular matrix. Thus, actin filaments of stress fibers indirectly Join to the inner face of the plasma membrane through molecular assemblies of attachment proteins, which include an actin-capping protein, a-actinin, vinculin, and talin (Small, 1988). 

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