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PubMed2003

An intact actin-containing cytoskeleton is required for capacitative calcium entry, but not for ATP-induced calcium-mediated cell signaling in cultured human keratinocytes.

BACKGROUND: The present study was focused on structural relationship between intracellular calcium stores and plasma membrane store-operated calcium channels in cultured normal and NF1 keratinocytes. MATERIAL/METHODS: Calcium mobilization induced by thapsigargin or extracellular ATP was studied in control and cytochalasin D-treated human keratinocytes. RESULTS: Treatment of keratinocytes with cytochalasin D disrupted the actin cytoskeleton and changed the cells from a planar, extended morphology, to a rounded shape. In normal control keratinocytes, thapsigargin induced a marked increase in intracellular calcium concentration ([Ca2+]i). The capacitative calcium influx of cytochalasin D-treated normal keratinocytes was significantly weaker compared to normal control cells. In normal keratinocytes, ATP induced a rapid and transient increase in [Ca2+]i. Thus disruption of the cytoskeleton blocked thapsigargin-induced calcium mobilization, but had no effect on ATP-induced [Ca2+]i mobilization in keratinocytes. The results suggest that microfilaments play crucial role for functional capacitative Ca2+ entry in cultured keratinocytes. The cytoskeleton and calcium mediated cell signaling have been demonstrated to be abnormal in keratinocytes cultured from patients with neurofibromatosis type 1 (NF1). In NF1 keratinocytes, thapsigargin induced a slow and moderate increase in [Ca2+]i. The effect of cytochalasin D on NF1 keratinocytes was less pronounced compared to normal keratinocytes. In NF1 keratinocytes, ATP induced a rapid and transient increase in [Ca2+]i. CONCLUSIONS: The actin microfilaments play a crucial role for functional capacitative Ca2+ entry in cultured keratinocytes, and that aberrant organization of cytoskeleton may partly explain altered calcium-mediated cell signaling in NF1.

Actins↗
PubMed2004

[Surface architectonics and cytoskeleton of erythrocytes and their modulation by adrenergic agents in patients with bronchial asthma].

AIM: To evaluate erythrocyte surface architectonics and cytoskeleton in bronchial asthma (BA) under modulation of adrenergic agents. MATERIAL AND METHODS: 24 healthy persons, 61 patients with bronchial asthma (BA) were examined. Of them, 28 patients had allergic BA (ABA) and 33 ones had nonallergic BA (NABA). Erythrocyte surface architectonics was studied by phase-contrast microscopy. Fixation in 0.5% solution of glutar aldehyde was used, preparation "squashed drop" was prepared. In all preparations adrenalin hydrochloride and obzidan were used in equimolar final concentrations of 4.10(-5) M. The mean morphologic index of transformation that reflects the shift to stomatocytosis or to echinocytosis was estimated to characterize integrally erythrocyte surface architectonics. The cytoskeleton was studied by the modified method of Chentosov's et al. The integral optic density was evaluated on imaging analyzer of Ista-Videotest company (St-Petersburg). RESULTS: In healthy persons there was a correlation between erythrocyte surface architectonics and cytoskeleton under modulation of adrenergic system. Adrenalin-induced decrease of cytoskeletal proteins correlated with the shift to stomatocytosis. In NABA erythrocyte surface architectonics was characterized by a pronounced shift to stomatocytosis. This shift was accompanied with the most pronounced decrease of cytoskeletal proteins and it reduced in remission. In ABA manifestation of the shift was minimal and did not depend on the phase of the disease. In ABA no changes in erythrocyte surface architectonics in the presence of adrenalin were revealed. In the same conditions a decrease in cytoskeletal proteins was found. CONCLUSION: A correlation was found between erythrocyte surface architectonics and cytoskeleton in healthy persons. In ABA, under modulation of adrenergic system by adrenalin dissociation was revealed between receptor and cytoskeletal mechanisms of cell form induction. This dissociation does not depend on the phase of the disease and is thought to be one of the important postreceptor disorders typical for this variant of the disease.

Adrenergic beta-Antagonists↗
PubMed2005

[Role of Rho kinase in reorganization of the vascular endothelial cytoskeleton induced by rat burn serum].

OBJECTIVE: To investigate the changes in endothelial cytoskeletal reorganization and the role of Rho in the signal transduction pathway. METHODS: ECV304 cells were cultured and randomly divided into following groups: i.e. sham (with normal rat serum treatment), burn (with burn rat serum treatment), Y (with 30 micromol/L Rho kinase inhibitor Y-27632 treatment), burn plus Y (pretreatment of cells with burn serum before treated with 30 micromol/L Y-27632), Y plus burn (pretreatment of cells with Y-27632 for 1 hour before treated with burn serum), LPA (with normal rat serum and 13 micromol/L LPA), and LPA plus Y (pretreatment of cells with LPA before treated with Y-27632) groups. The indices were examined at 6, 7 and 8 posttreatment hours (PTH) in all groups except in Y group. The endothelial morphology was observed with HE staining. Endothelial cytoskeleton was observed by dual-fluorescence labeling of filamenta (F) with Rhodamine-phalloidin and monomer (G) with oregon green labeled DNAase. The actin content in the cells in all groups was measured with flow cytometry. RESULTS: In sham and control group, the cells were in fusiform or polygonal shape, with satisfactory growth; filamentous actin (F-actin) was mainly distributed in the peripheral site of the cytoplasm and formed peripheral filamental band. The cells became confluent to form a single layer with reticular structure. Globular actin (G-actin) was concentrated in the nucleus and per nucleus. In burn group, after 6 hours of burn serum treatment, the ability of cells to adhere to vessel wall was weakened, and a striking reorganization of the actin cytoskeleton and the formation of the stress fibers were found. Furthermore, the fluorescent intensity of the peripheral filament bands was weakened, and dispersed actin monomers were seen in the cytoplasm. This reaction was enhanced along with elapse of stimulation time. In burn plus Y or Y plus burn group, the cells grew and adhered well to the wall of culture vessel. The distribution of the filamentous actin was the same as the sham group, while the stress fiber decreased in amount obviously. The structure of globular actin was condensed with little G-actin in the cytoplasm. The changes in actin cytoskeleton in LPA group was similar to that in burn group. The effects of LPA on actin reorganization could also be reversed by Y-27632. The content of F-actin in burn group at 6 PTH (0.63 +/- 0.07) was lower than that in sham group (0.75 +/- 0.08), while the content of G-actin in burn group (1.28 +/- 0.27) was higher than that in sham group (1.16 +/- 0.16, P > 0.05). CONCLUSION: Burn serum induces vascular endothelial actin cytoskeleton reorganization in endothelial cells via the Rho-dependent signal pathway. Similar to the effect of LPA, this effect could be reversed by Y-27632.

Actins↗
PubMed1992

Organization of cortical cytoskeleton of cultured chromaffin cells and involvement in secretion as revealed by quick-freeze, deep-etching, and double-label immunoelectron microscopy.

We have studied the organization of the cytoskeleton in both unstimulated and stimulated cultured chromaffin cells, as well as its relationship with their secretory process by exocytosis. We found the spatial heterogeneity in the intensity of cortical rhodamine-phalloidin staining within a cell. The overall staining pattern or intensity was minimally altered after stimulation, although dopamine-beta-hydroxylase (DBH) antigen, a marker for the chromaffin granule membrane, was exposed preferentially on the plasma membrane areas with lower intensity of rhodamine-phalloidin staining. Using the quick-freeze, deep-etch technique, we found the heterogeneity in the organization of cortical cytoskeletal networks--some regions have actin filament bundles running parallel to the plasma membrane interspersed between granules and the plasma membrane, while others have few actin filaments beneath the plasma membrane before stimulation. Actin filaments were rarely observed in the inner cytoplasm. We did not observe the overall change in its organization after stimulation. Double-label immunogold EM using anti-DBH antibody and anti-actin antibody combined with statistical analysis showed that (1) DBH was exposed on the plasma membrane preferentially where actin was sparse after stimulation (significant at less than 0.1%), although (2) regions having sparse actin were not always the sites for DBH exposure, and (3) the cortical actin zone was sometimes disrupted at the DBH-exposed sites after stimulation. The present data suggested that (1) secretion is related to heterogeneous organization of cortical cytoskeleton after stimulation and (2) massive synchronized reorganization of the cytoskeleton in the whole cell is not necessary for secretion, although small changes of the cytoskeleton might occur under local regulation at each exocytotic site at the moment of the release.

Actins↗
PubMed2006

[Development of a novel in-vitro culture device simulating distraction osteogenesis and expression of osteoblast cytoskeleton].

OBJECTIVE: To establish a novel in-vitro culture device simulating distraction osteogenesis, and to understand the the changes of cytoskeleton of osteoblasts under different magnitudes of mechanical distraction. METHODS: A novel in-vitro culture device simulating distraction osteogenesis was developed with titanium and silicon membrane. The expressions of F-actin cytoskeleton subjected to different magnitudes of distraction were observed in situ under a confocal laser scanning microscope, and protein levels of actin and tubulin alpha were analyzed by electrophoresis of Western blot. RESULTS: The mode of culture device simulating distraction osteogenesis was similar to that of distraction osteogenesis used in clinic. After 24 h mechanical distraction with physiological magnitude, F-actin of osteoblasts was organized and paralleled to the direction of distraction forces. After 24 h mechanical distraction with hyperphysiological magnitude, however, F-actin of osteoblasts became reorganized and disrupted, and protein levels of actin and tubulin alpha decreased. CONCLUSIONS: The novel in vitro culture device simulating distraction osteogenesis is suitable for the study of distraction osteogenesis in vitro. Physiological mechanical distraction causes organization and rearrangement of actin cytoskeleton. However, hyperphysiological mechanical distraction results in reorganization and disruption of actin cytoskeleton.

Actins↗
PubMed2006

[Dynamics of microtubular cytoskeleton in higher plant meiosis. IX. The cycle accomplishment. Transition from phragmoplast to radial microtubule system].

In this study we analysed the terminal step of cytoskeleton cycle in higher plant meiosis: transition from phragmoplast to radial interphase configuration. Wild type meiosis in a range of mono- and dicotyledonous species was studied. A number of cytoskeleton abnormalities on this stage was described in meiotic mutants, haploids and wide hybrids of various species. We described processes of cytoskeleton rearrangements on this stage: disjunction of phragmoplast MTs, their shortening and the role of daughter cell membranes. The independence of the interphase radial MT system formation from the previous steps of cytoskeleton cycle and from nuclear envelope cycle is proposed.

Chimera↗
PubMed1991

Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets.

Phosphatidylinositol (PtdIns)-4- and -3-kinases, PtdIns(4)P-5-kinase, diacylglycerol (DAG) kinase, and PtdIns-phospholipase C were all detected in cytoskeletons of resting human platelets. The total cytoskeletal enzyme activities were greatly increased upon thrombin stimulation of the intact cells. Those reached a maximum after a 60-s stimulation for PtdIns(4)P-5-kinase and phospholipase C, while the other kinases appeared to be slightly delayed. Specific activities were stimulated from about 4-fold (PtdIns-3-kinase) to about 6-fold (PtdIns-4-kinase). Thrombin treatment also promoted a co-extraction of pp60c-src with the cytoskeletons and its disappearance from the Triton X-100 soluble fraction. These results suggest that stimulation of platelets by thrombin causes the association of enzymes responsible for lipid phosphorylation and hydrolysis with the cytoskeletons. This could occur at cytoskeleton anchoring points to the membranes.

1-Phosphatidylinositol 4-Kinase↗
PubMed1991

Structural and chemical changes in the cytoskeleton of the goldfish Mauthner cells after vestibular stimulation.

The ultrastructure and protein content of goldfish Mauthner cells (M-cells) at different functional states induced by natural vestibular stimulations were studied. 2-h stimulation, usually causing a fatiguing of the fishes, was found to be accompanied by ultrastructural changes within M-cells and a decreased content of cytoskeletal proteins. After training by short stimulations resulting in a long-term adaptation of the fishes, the ultrastructure and protein content of M-cells could not be distinguished qualitatively and quantitatively from those of non-adapted fishes. When the adapted fishes were stimulated for 2 h the content of a 70-kDa protein was found to be increased. In addition, the content of a 42-kDa protein, obviously actin, was elevated in this case. Correspondingly, electron microscopic analysis demonstrated a significantly increased resistance of the cytoskeleton to fatiguing stimulation. The data obtained indicate that the neural cytoskeleton is a central target of fatiguing stimulation. We suppose that the 70-kDa protein is responsible for the adaptive properties of the cytoskeleton. This protein is assumed to be identical with one of the so-called heat-shock proteins of non-neural cells which have the same electrophoretic mobility and are also able to protect the cytoskeleton under stress conditions.

Acoustic Stimulation↗
PubMed1991

Alterations in the cytoskeleton of the goldfish Mauthner cells under various pharmacological treatments.

The ultrastructural changes in the cytoskeleton of the goldfish Mauthner cells (M-cells) at various functional states induced by intracerebral microinjections of biologically active substances were studied. Under the action of kainic acid, a structural analog of the excitatory neurotransmitter of glutamate, the density of the cytoplasmic matrix increased. Cytotoxin II from the cobra toxin, which blocks acetylcholine transmission, had an opposite effect upon the M-cell cytoskeleton. Simultaneously, in some areas of the neural cytoplasm strands of an electron-dense material of various shapes appeared. They had an unique structure which did not resemble any known cytoskeleton element. The molecular composition of the strands is unknown, but similar strands appeared after injections of phalloidin or cytochalasin B, both disturbing the microfilamental component of the cytoskeleton. Decoration with myosin subfragment-1 revealed actin in intact M-cells which was organized as crossing loose filaments and bundles of parallel fibers. The morphology of the fiber bundles resembles the helical part of the strands appearing after the treatment with phalloidin, cytochalasin B, or cytotoxin II. It is suggested that the cytoplasmic matrix of M-cells is a dynamic system which responds to the functional changes by thickening or loosening of its cytoskeletal elements or by formation of new structures.

Acoustic Stimulation↗
PubMed1991

Hyperexpression of interferon-gamma-induced MHC class II genes associated with reorganization of the cytoskeleton.

Class I and class II major histocompatibility complex (MHC) gene products are key recognition units in the induction and regulation of the immune response. Expression of class I and class II may be constitutive or inducible by cytokines such as interferon-gamma (IFN-gamma). A key step in the induction of MHC genes is recognition of IFN-gamma by its membrane receptor. The work described here examines the regulation of the occupied IFN-gamma receptor by the cytoskeleton. To do this the authors have used the fungal metabolites dihydrocytochalasin B (DHCB) and cytochalasin D (CD), substances that bind to actin filaments and thereby disrupt the cytoskeleton. The authors have studied the effect of DHCB and CD on IFN-gamma-induced MHC gene expression in 143 B cells, a human osteosarcoma-derived cell line. Herein the authors demonstrate that alterations in the cytoskeleton induced by DHCB and CD can lead to increases in IFN-gamma-induced MHC gene expression. Dihydrocytochalasin B added up to 3 hours after IFN-gamma results in a threefold to sixfold increase in levels of class II mRNA while producing minimal enhancement of class I gene expression. In contrast, glyceraldehyde-3-phosphate dehydrogenase mRNA expression was unaltered by IFN-gamma or by the cytochalasins. The increased amount of class II mRNA can be accounted for by a concomitant increase in transcription rate of this gene. Studies using 125I-IFN-gamma demonstrate that the occupied IFN-gamma receptor associates with a Triton X-100 insoluble fraction of 143 B cells and that DHCB and CD markedly inhibit this association. The results described here provide evidence that is consistent with the hypothesis that the activity of the occupied IFN-gamma receptor may be modulated by interactions with the cytoskeleton of the cell. This receptor may be one of a group of plasma membrane receptors that are sensitive to the action of cytochalasins after ligand binding.

B-Lymphocytes↗
PubMedDate not supplied

[The cytoskeleton and mechanoreception thresholds].

In order to analyse the mechanisms of high sensitivity of mechanoreceptors the role of cytoskeleton in the deformation of receptor membrane was considered. The later was considered as an elastic plate. Local relative deformations epsilon s near the attachment points of cytoskeleton filaments to the membrane were calculated. It is shown that at different types of deformation for small regions of the membrane with the size R of several scores of nm the epsilon s values are L/R where L is absolute displacement of the region under the effect of the force applied. For the hair cells of the corti organ the model including neighbor stereocilia connected by the skeleton filaments shows the values epsilon s approximately 10(-4). The latter by several orders exceed the values characteristic of the single stereocilium deflection. On the basis of the model calculations of epsilon s a hypothesis is advanced for Pacinian corpuscle concerning the existence of a bond between the membrane sensitive ending and the inner capsula via cytoskeleton filaments, which suggests high epsilon s values of this receptor. The cytoskeleton elements should be considered an intrinsic part of the sensitive centre.

Animals↗
PubMed1986

Cross-linking of immunoglobulin E-receptor complexes induces their interaction with the cytoskeleton of rat basophilic leukemia cells.

Bridging of immunoglobulin E (IgE)-receptor complexes on rat basophilic leukemia cells by polyclonal anti-IgE antibodies induces a detergent-resistant association of these complexes with the cellular cytoskeleton. In dose-response curves the extent of the cytoskeletal association appears to follow the extent of bridging, continuing to increase beyond where stimulated degranulation is maximal. This stable association is maintained after the aggregated IgE-receptor complexes have been internalized by the cell. Multivalent antigen and trimeric IgE cause less extensive receptor cross-linking than anti-IgE and stimulate degranulation; they also induce receptor association with the cytoskeleton that is revealed only after stabilization by addition of a chemical cross-linking reagent. The ability of a membrane impermeant chemical cross-linker to stabilize this association suggests that the receptor-cytoskeletal interaction may be mediated by a transmembrane protein that is exposed at the cell surface. Monomeric and dimeric IgE bound to receptors fail to induce a stable interaction with the cytoskeleton even in the presence of chemical cross-linkers and are poor (dimers) or insignificant (monomers) stimulators of cellular degranulation. These findings are consistent with a possible relationship between receptor attachment to the cytoskeleton, receptor immobilization as measured by fluorescence photobleaching recovery, and the triggering of cellular degranulation.

Animals↗
PubMed1989

Problems associated with the preparation of whole mounts of cytoskeletons for high resolution electron microscopy.

The resolution currently available in both transmission and scanning electron microscopes is theoretically adequate to visualize the organization of the cytoskeleton at the supramolecular and macromolecular levels. However, achieving this resolution in practice requires that the methods used to prepare the specimens both preserve the structures of interest and render them visible for observation in the microscope without obscuring or altering them. In this paper we discuss our own and others efforts to develop methods to overcome several problems associated with preparing whole mounts of cytoskeletons for observation by electron microscopy. These problems include: controlling the degree to which cellular components are extracted; the effects of osmium tetroxide on the cytoskeleton; controlling and recognizing shrinkage and drying artifacts; the choice of a method of visualization; deposition of grain-free ultrathin films of metal; and interpreting the results. The standard procedure which we currently use consists of the following steps: growing cells on carbon-stabilized Formvar-coated gold electron microscope grids; extracting in 0.5% Triton X-100 detergent in a microtubule stabilizing buffer; postfixing in 2.5% glutaraldehyde in stabilizing buffer; freeze-drying; magnetron sputter-coating with 1.5 nm of tungsten; and observation by TEM, SEM, or STEM. Cytoskeletons prepared in this manner contain over 100 polypeptides and are composed of a complex three dimensional meshwork of clean, uniform filaments, the smallest of which are 7 nm in diameter. A structure resembling the microtrabecular lattice is present only if the cells are prefixed with a relatively long bifunctional protein crosslinking reagent prior to extraction with detergent.

Animals↗
PubMed1979

The cytoskeleton and cytomusculature in embryogenesis--an overview.

The role of microfilaments and microtubules comprising the cytoskeleton and cytomusculature in embryonic development is discussed. The cytomusculature, as microfilaments, is evident in both the unfertilized and fertilized egg and probably plays a role in sperm incorporation, cortical contractions, and cytokinesis. The cytoskeleton, in the form of microtubules, appears after fertilization in the form of the sperm aster and the mitotic apparatus. The cytoskeleton and cytomusculature play a decisive role in shape changes of individual cells responsible for gastrulation, neurulation, and morphogenesis of other epithelial sheets. Several developmental defects, such as spina bifida, may be related to malfunctioning of the cytoskeleton or cytomusculature. The putative role of microfilaments and microtubules in cell shape changes during embryogenesis can best be, at least initially, inferred from careful ultrastructural observations.

Animals↗
PubMed1986

The cytoskeleton of the cynomolgus monkey trabecular cell. I. General considerations.

Many cellular functions involve the complex network of actin filaments, microtubules, and intermediate filaments collectively known as the cytoskeleton. Stereo transmission electron microscopic observations of whole cynomolgus monkey trabecular cells, which were extracted, S-1 labeled, and critical-point dried, were employed to simultaneously identify these three major cytoskeletal systems and visualize their three-dimensional nature. A double fluorescence technique for actin and microtubules was used to provide a broad view of cytoskeletal relationships within the cell. Actin microfilaments were the most prominent elements of the cytoskeleton. They appeared as bundles in stress fibers. Between stress fiber bundles, a continuous meshwork of microfilaments and intermediate filaments could be seen. Numerous microtubules radiated from the centriole region to the cell periphery. This comprehensive overview of the cytoskeleton of the cynomolgus monkey trabecular cell can be used to understand structure-function relationships of the trabecular cell cytoskeleton and its influence on outflow facility.

Actins↗
PubMed1981

The application of scanning electron microscopy to the study of the cytoskeleton of cells in culture.

This paper reviews the methods available for studying the structural organization of the cytoskeleton of cells in culture. These are transmission electron microscopy of whole cells, immunofluorescence, and detergents extraction procedures. Published methods for detergent extraction are critically reviewed with special emphasis on those factors that are most relevant for the preparation of cytoskeletons for observation by scanning electron microscopy. These include the type of detergent, the use of chemical crosslinking reagents or specially formulated buffers to stabilize the cytoskeleton during extraction, the osmotic and salt composition of the extraction medium, the use of cool sputter coaters, and the application of minimal amounts of metal during coating. Finally, examples are given of the types of information about the three dimensional organization of the cytoskeleton that can be obtained by SEM.

Animals↗
PubMed1983

Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells.

Plectin (Mr = 300,000) was found to be an abundant polypeptide component of Chinese hamster ovary cells accounting for up to 1% of cellular protein. Seventy-five per cent of the plectin were present in cytoskeletons prepared by extraction of attached cells with 0.15% Triton X-100. As shown by immunofluorescence microscopy, plectin's spatial arrangement within these cytoskeletal preparations appeared well preserved, though slightly more filamentous compared to nonextracted cells. Upon in situ incubation of cytoskeletons with [gamma-32P] ATP followed by solubilization and immunoprecipitation, plectin was identified as one of the major phosphoacceptors. A basic phosphorylation of the protein was accomplished by a type I cAMP-independent protein kinase, while a cAMP-dependent protein kinase enhanced its phosphorylation up to 2-fold. Peptide mapping revealed that the two kinases phosphorylated different molecular sites. Peptide maps generated from cytoskeletal plectin phosphorylated in vitro using [gamma-32P]ATP and plectin phosphorylated in vivo using 32Pi were virtually identical demonstrating that the in situ phosphorylation of plectin in preparations of cytoskeletons was specific. Moreover, the specific radioactivity of cytoskeletal plectin was three times higher than that of detergent-extracted plectin, suggesting that phosphorylation is important for the protein's association with the cytoskeleton.

Animals↗
PubMed1995

Neurofibromatosis type 2 protein co-localizes with elements of the cytoskeleton.

The product of the neurofibromatosis type 2 (NF2) tumor suppressor gene is a 595-amino-acid protein bearing resemblance to a family of band-4.1-related proteins. These proteins, including ezrin, radixin, and moesin, probably function as molecular linking proteins, connecting the cytoskeleton to the cell membrane. On the grounds of the homology to the ezrin, radixin, and moesin proteins and on the basis of its predicted secondary structure, the NF2 protein is also thought to act as a cytoskeleton-cell membrane linking protein. Using monoclonal antibodies to amino- and carboxyl-terminal synthetic NF2 peptides we demonstrate the co-localization of the NF2 protein with elements of the cytoskeleton in a COS cell model system and in cultured human cells. Furthermore, the presence of the NF2 protein in tissue sections is shown. The monoclonal antibodies specifically stain smooth muscle cells and the stratum granulosum of the human epidermis. In cultured smooth muscle cells the NF2 protein co-localizes with actin stress fibers. Immunoelectron microscopy demonstrates the presence of the NF2 protein associated with keratohyalin granules and to a lesser extent with intermediate filaments in the human epidermis. We conclude that the NF2 protein is indeed associated with multiple elements of the cytoskeleton.

Actins↗