..., mechanotransduction and gene regulation. However, the mechanisms that underlie these processes are not well known. Skeletal muscle cells provide a convenient system to understand IF function because the major muscle-specific IF, desmin, is expressed in high abundance and is highly organized. Here, we show that desmin...

... of Biologists Ltd 2014 Desmin Muscle hypertrophy Intermediate filament Skeletal muscle Intermediate filaments (IFs) are filamentous components of the cytoskeleton of 10-nm diameter that mechanically connect various structures of the cytoplasmic space (Lazarides, 1980). The tissue- or cell-type...

...Gloria M. Conover; Carol C. Gregorio Desmin intermediate filaments intimately surround myofibrils in vertebrate muscle forming a mesh-like filament network. Desmin attaches to sarcomeres through its high-affinity association with nebulin, a giant F-actin binding protein that co-extends along...

...Michele R. Stone; Andrea O'Neill; Richard M. Lovering; John Strong; Wendy G. Resneck; Patrick W. Reed; Diana M. Toivola; Jeanine A. Ursitti; M. Bishr Omary; Robert J. Bloch Intermediate filaments, composed of desmin and of keratins, play important roles in linking contractile elements to each other...

... muscle cells. The desmosomal component desmoplakin plays a key role in tethering various intermediate filament networks through its C-terminal plakin repeat domain. To gain better insight into the cytoskeletal organization of cardiomyocytes, we investigated the association of desmoplakin with desmin...

...Susan C. Schweitzer; Michael W. Klymkowsky; Robert M. Bellin; Richard M. Robson; Yassemi Capetanaki; Robert M. Evans ABSTRACT De novo expression of vimentin, GFAP or peripherin leads to the assembly of an extended intermediate filament network in intermediate filament-free SW13/cl.2 cells. Desmin...

..., we investigated whether the muscle-specific intermediate filament protein desmin would be able to functionally complement a mutant keratin 14 in cultured keratinocytes. We show that in stably transfected EBS cells, desmin forms an extended keratin-independent cytoskeleton. Immunogold-EM analysis...

.... Immunofluorescence analysis revealed that plectin was colocalized with desmin at the periphery of Z-discs. This plectin localization around Z-discs was constantly maintained irrespective of the contracted or extended state of the muscle fibers, suggesting either direct or indirect association of plectin with Z-discs...

... the longer length version with an extra 42 residues. St-A is the first IF protein from a lower chordate which can be unambiguously related to a particular vertebrate IF subfamily. St-A shares 46% sequence identity with desmin, displays the N-terminal motif necessary for filament assembly of type III proteins...

..., while in proliferating myoblasts of the C2.7 mouse myogenic cell line the prosomal antigens seem to superimpose on the intermediate filaments of the desmin type. Thus, the prosomes, which are RNP particles of variable composition and subcomplexes of untranslated mRNP, and carry a multicatalytic...

... head domain of desmin is structurally closely related to that of vimentin (Geisler et al. 1982 ; Fischer et al. 1986) and both IF proteins can assemble into heteropolymeric filaments (Steinert et al. 1981b; Quinlan and Franke, 1982), both head domains were expected to exert very similar effects...

... microscopy experiments on whole-mount chick embryo cells and showed that IFAPa-400 was localized at crossing points of intermediate filaments. Also, immunoblot experiments with F51H2, anti-vimentin and anti-desmin antibodies demonstrated the complete disappearance of IFAPa-400 in those muscle cell types...

.... In immunoblots on conduction tissue homogenates the two antibodies recognized two polypeptides with electrophoretic mobility and solubility properties identical to those of NF-L and NF-M in the sciatic nerve. The subcellular distribution of NF immunoreactivity in specialized myocytes was very similar to desmin...