Recent insights into the assembly, dynamics, and function of intermediate filament networks

Skalli, Omar; Goldman, Robert D.

doi:10.1002/cm.970190202

Cited by 148 publications

(65 citation statements)

References 177 publications

(91 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A similar situation was not applicable to the smooth muscle cells. Generally speaking, some additional functional significances for intermediate filaments were proposed; they may be involved in conveying mechanical information from the cell surface to the nucleus, in aligning T-tubules to the Z-discs, in anchoring cell organelles in the cytoplasm, forming a perinuclear network, and in directing specific mRNA to specific locations in cells (Lazarides, 1980;Skalli and Goldman 1991;Wang et al, 1993). The exact functional significances of the intermediate filament system in smooth muscle are not known, though it associates with the dense plaques at the cell surface.…”

Section: Discussionmentioning

confidence: 99%

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Tanaka

Hijikata

Murakami

et al. 2001

Cell Struct. Funct.

View full text Add to dashboard Cite

ABSTRACT. Plectin is a versatile linker protein which is associated with various types of cytoskeletal components and/or filaments including intermediate filaments. To better understand the functional roles of plectin in smooth muscle cells, we examined the distribution of plectin and other related proteins in rat colon smooth muscles by confocal laser and electron microscopy. The sarcolemma of smooth muscle cells exhibits two ultrastructurally distinct domains, domains associated with dense plaques and caveola-rich domains. Staining with anti-plectin and anti-desmin antibodies showed that plectin was localized along the sarcolemma in an intermittent manner and desmin was distributed in the sarcoplasm and intermittently at the cell periphery where it was codistributed with desmin. Plectin exhibited complementary and non-overlapping distribution to caveolin-1 and dystrophin, components of caveola domains, whereas plectin was codistributed with vinculin, talin and integrin > > > >1, components of dense plaques. Plectin was also codistributed with > > > >2-chain laminin but not with > > > >1-chain laminin. Electron microscopic observations on the sarcolemma revealed close association of intermediate filaments with dense plaques. Correlated confocal and electron microscopy clearly demonstrated that anti-plectin fluorescence corresponded to dense plaques but not to caveola domains in electron microscopic images. These findings indicate that plectin is confined to dense plaques to which desmin intermediate filaments may be anchored in rat colon smooth muscle cells.Key words: smooth muscle/plectin/dense plaques/confocal laser microscopy/electron microscopy/caveolin-1 Plectin, a member of the plakin family, is a versatile cytoskeletal linker protein and occurs in a wide variety of tissues and cell types, in which plectin codistributes with various types of intermediate filament proteins, such as vimentin, cytokeratins, desmin and glial fibrillary acidic (GFA) protein (Wiche et al., 1983Hieda et al., 1992;Errante et al., 1994;Yaoita et al., 1996;Svitkina et al., 1996;Eger et al., 1997;Foisner et al., 1988Foisner et al., , 1991. Plectin is located at the intermediate filament-plasma membrane interface, such as hemidesmosomes, desmosomes, and cardiac muscle intercalated discs. Plectin appears to act as molecular bridges between intermediate filaments and actin filaments or microtubules, as shown by whole-mount electron microscopy (Wiche et al., 1982(Wiche et al., , 1983. More recently, plectin has been shown to link intermediate filaments to the Z-discs in skeletal muscle fibers (Hijikata et al., 1999). Consistent with these variable locations, plectin possesses the binding capacity to multiple cytoskeletal proteins, such as =-spectrin (fodrin), high molecular mass microtubule-associated proteins and integrin >4 (Hermann and Wiche, 1987;Svitkina et al., 1996;Rezniczek et al., 1998). The strategic localization and versatile binding property of plectin suggest that it plays significant functional roles in the structural inte...

show abstract

Section: Discussionmentioning

confidence: 99%

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Tanaka

Hijikata

Murakami

et al. 2001

Cell Struct. Funct.

View full text Add to dashboard Cite

show abstract

“…Second, we consider how specializations of polypeptide structure and posttranslational modifications unique to neurofilaments may have evolved to stabilize the filament network and to serve better the purposes of the highly polar, postmitotic neuron. Some aspects of these themes have been reviewed recently [Julien and Grosveld, 1991;Nixon, 1991;Shaw, 1991;Skalli and Goldman, 1991;Steinert and Roop, 19881.…”

Section: Introductionmentioning

confidence: 99%

Dynamics of neuronal intermediate filaments: A developmental perspective

Nixon

Shea

1992

Cell Motil. Cytoskeleton

217

159

View full text Add to dashboard Cite

mentioning

confidence: 99%

“…It has been shown that phosphorylation is a principal factor in the regulation of intermediate filament (IF) polymerization, subcellular organization, and dynamics (1,2). IF proteins are substrates for several different kinases, including p34cdc2 kinase (1,2). In the latter case, hyperphosphorylation of vimentin-containing IF is directly correlated with their disassembly into protofilamentous structures (3)(4)(5).…”

mentioning

confidence: 99%

Cytoskeletal integrity in interphase cells requires protein phosphatase activity.

Eriksson

Brautigan

Vallee

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

151

View full text Add to dashboard Cite

Phosphorylation by protein kinases has been established as a key factor in the regulation of cytoskeletal structure. However, little is known about the role of protein phosphatases in cytoskeletal regulation. To assess the possible functions ofprotein phosphatases in this respect, we studied the effects of the phosphatase inhibitors calyculin A, okadaic acid, and dinophysistoxin 1 (35-mnethylokadaic acid) on BHK-21 fibroblasts. Within minutes of incubation with these inhibitors, changes are seen in the structural organization of intermediate filaments, followed by a loss of microtubules, as assayed by immunofluorescence. These changes in cytoskeletal structure are accompanied by a rapid and selective increase in vimentin phosphorylation on interphase-specific sites, and they are fully reversible after removal of calyculin A. The results indicate that there is a rapid phosphate turnover on cytoskeletal intermediate filaments and further suggest that protein phosphatases are essential for the maintenance and structural integrity of two major cytoskeletal components.

show abstract

Recent insights into the assembly, dynamics, and function of intermediate filament networks

Cited by 148 publications

References 177 publications

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Localization of Plectin and Other Related Proteins along the Sarcolemma in Smooth Muscle Cells of Rat Colon.

Dynamics of neuronal intermediate filaments: A developmental perspective

Cytoskeletal integrity in interphase cells requires protein phosphatase activity.

Contact Info

Product

Resources

About