Intermediate filament proteins in nonfilamentous structures: Transient disintegration and inclusion of subunit proteins in granular aggregates

Franke, Werner W.; Schmid, Erika Nardon; Gründ, Christine; Geiger, Benjamin

doi:10.1016/0092-8674(82)90016-2

Cited by 246 publications

(129 citation statements)

References 53 publications

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“…5 demonstrates the reorganization of keratin in an untreated dividing HeLa cell . The spheroidal bodies (15,16) stain intensely with antikeratin antiserum .…”

Section: Resultsmentioning

confidence: 99%

“…SAWYER Department of Biology, University of South Carolina, Columbia, South Carolina 29208 function (6) . Recent immunofluorescence studies of cytokeratins during mitosis in certain epithelial cell types, including HeLa cells, have demonstrated that the otherwise immutable organization of cytokeratins changes from an extended filamentous arrangement to a condensed, spheroidal form as the cells divide, with the re-establishment of extended filaments following division (15,16). This transformation suggests that there are specific mechanisms for the alteration of cytokeratin organization that may be dependent on, or triggered by, changes in the organization of microfilaments and microtubules.…”

mentioning

confidence: 99%

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Rearrangement of the keratin cytoskeleton after combined treatment with microtubule and microfilament inhibitors.

Knapp¹,

O’Guin²,

Sawyer³

1983

The Journal of Cell Biology

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In addition to containing microtubule and microfilament systems, vertebrate epithelial cells contain an elaborate keratin intermediate-filament cytoskeleton . Little is known about its structural organization or function . Using indirect immunofluorescence microscopy with an antikeratin antiserum probe, we found that destabilization of microtubules and microfilaments with cytostatic drugs induces significant alterations in the cytoskeletal organization of keratin filaments in HeLa and fetal mouse epidermal cells . Keratin filament organization was observed to undergo a rapid (1-2 h) transition from a uniform distribution to an open lattice of keratin fibers stabilized by membrane-associated focal centers . Since addition of any one drug alone did not elicit significant organizational change in the keratin cytoskeleton, we suggest that microfilaments and microtubules have a combined role in maintaining the arrangement of keratin in these cells . Vimentin filaments, the only other intermediatesized filaments found in HeLa cells, did not co-distribute with keratin in untreated or drugtreated cells . These findings offer a new way to approach the study of the dynamics and functional roles of the keratin cytoskeleton in epithelial cells .

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“…5 demonstrates the reorganization of keratin in an untreated dividing HeLa cell . The spheroidal bodies (15,16) stain intensely with antikeratin antiserum .…”

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Rearrangement of the keratin cytoskeleton after combined treatment with microtubule and microfilament inhibitors.

Knapp¹,

O’Guin²,

Sawyer³

1983

The Journal of Cell Biology

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“…Like those of vimentin, the phosphorylation levels of the keratins are elevated in mitosis, and the organizational fates of keratin IF networks vary from one cell type to another (Horwitz et al, 1981;Franke et al, 1982;Lane et al, 1982;Celis et al, 1983;Ku and Omary, 1994). It is therefore likely that variations in the disassembly of keratin IFs observed in different types of epithelial cells are also regulated by keratin phosphorylation, along with the expression of unique keratin-associated proteins (Fuchs and Karakesisoglou, 2001;Leung et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…In PtK-2 epithelial cells, both vimentin and keratin IF networks remain intact during mitosis (Aubin et al, 1980). In HeLa cells, which also possess keratin and vimentin networks, the keratin network is disassembled into spheroid bodies, whereas vimentin remains filamentous (Franke et al, 1982;Jones et al, 1985). The various organizational fates of cytoplasmic IFs in different cell types undergoing mitosis suggest that the biochemical factors regulating their restructuring during mitosis are not identical.…”

Section: Introductionmentioning

confidence: 97%

“…The phosphorylation of vimentin by MPF is a universal feature of mitotic cells expressing vimentin. Yet the breakdown of vimentin networks during mitosis has been reported only in MDBK (Franke et al, 1982), BHK-21 (Rosevear et al, 1990), and ST15A (Sahlgren et al, 2001) cells. Therefore, additional factors, unique to these three cell lines, are required for the disassembly of IFs.…”

Section: Introductionmentioning

confidence: 99%

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Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Chou

Khuon

Herrmann

et al. 2003

MBoC

173

153

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The expression of the intermediate filament (IF) protein nestin is closely associated with rapidly proliferating progenitor cells during neurogenesis and myogenesis, but little is known about its function. In this study, we examine the effects of nestin expression on the assembly state of vimentin IFs in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IFs into nonfilamentous aggregates or particles in mitotic but not interphase cells. This nestin-mediated disassembly of IFs is dependent on the phosphorylation of vimentin by the maturation/M-phase–promoting factor at ser-55 in the amino-terminal head domain. In addition, the disassembly of vimentin IFs during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is downregulated by the nestin-specific small interfering RNA in nestin-expressing cells, vimentin IFs remain assembled throughout all stages of mitosis. Previous studies suggest that nonfilamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. On the basis of these observations, we speculate that nestin may play a role in the trafficking and distribution of IF proteins and potentially other cellular factors to daughter cells during progenitor cell division

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Immunomicroscopy of neurofilaments in chromaffin cells of the adult bovine adrenal gland

et al. 1996

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Neurofilaments (NFs) represent a class of intermediate filaments which are highly specific for neurons. The most abundant of the native NFs is the 68 kD subunit (NF-L). Chromaffin cells of the adrenal medulla express NF subunits under culture conditions. However, NF expression in situ is questionable. It has been reported that as chromaffin cell precursors mature and begin to express catecholamine-synthesizing enzymes, their neuronal traits are extinguished and they become endocrine-like cells. This study reports that while NF-L may be lacking in the adrenal medulla of some species, NF-L immunoreactivity is clearly present in the adult bovine adrenal medulla. Immunofluorescence microscopy of bovine chromaffin cells in culture demonstrated NF immunoreactivity localized to both thin, highly ramified filaments present throughout the cell and frequently to an intensely immunofluorescent spot located near the nucleus. Double-label immunofluorescence microscopy and immunoblot analysis also demonstrated NF-L immunoreactivity in mature chromaffin cells of the bovine adrenal gland. In vitro and in situ immunofluorescence results were confirmed by immunogold and immunoperoxidase labelling, respectively. In both cases, NF-L immunoreactivity was associated with filaments in close proximity to the nucleus. Additionally, a spheroidal aggregate of immunogold-labelled NFs was seen adjacent to the nucleus in cultured cells. In conclusion, NF-L in bovine chromaffin cells demonstrates that at least one neuronal trait persists in these catecholamine-producing cells of the mature adrenal gland. In addition, this study emphasizes the fact that interspecies comparisons must be interpreted with caution, especially when attempting to formulate a generalized hypothesis.

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Intermediate filament proteins in nonfilamentous structures: Transient disintegration and inclusion of subunit proteins in granular aggregates

Cited by 246 publications

References 53 publications

Rearrangement of the keratin cytoskeleton after combined treatment with microtubule and microfilament inhibitors.

Rearrangement of the keratin cytoskeleton after combined treatment with microtubule and microfilament inhibitors.

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Immunomicroscopy of neurofilaments in chromaffin cells of the adult bovine adrenal gland

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