Nanomechanics of vimentin intermediate filament networks

Soft Matter ◽  
2010 ◽  
Vol 6 (9) ◽  
pp. 1910 ◽  
Author(s):  
Sarah Köster ◽  
Yi-Chia Lin ◽  
Harald Herrmann ◽  
David A. Weitz
Keyword(s):  
Intermediate Filament ◽  
Filament Networks ◽  
Vimentin Intermediate Filament

scholarly journals Stiffening and inelastic fluidization in vimentin intermediate filament networks

Soft Matter ◽  
2019 ◽  
Vol 15 (36) ◽  
pp. 7127-7136 ◽  
Author(s):  
Anders Aufderhorst-Roberts ◽  
Gijsje H. Koenderink
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Shear Rheology ◽  
Cellular Processes ◽  
Filament Networks ◽  
Nonlinear Shear ◽  
Vimentin Intermediate Filament

Nonlinear shear rheology reveals that intermediate filaments balance two contradictory roles: mechanoprotection by stiffening and dynamic cellular processes through softening.

Desmin and Vimentin Intermediate Filament Networks: Their Viscoelastic Properties Investigated by Mechanical Rheometry

2009 ◽  
Vol 388 (1) ◽  
pp. 133-143 ◽  
Author(s):  
Michael Schopferer ◽  
Harald Bär ◽  
Bernhard Hochstein ◽  
Sarika Sharma ◽  
Norbert Mücke ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Viscoelastic Properties ◽  
Filament Networks ◽  
Vimentin Intermediate Filament

scholarly journals Motile Properties of Vimentin Intermediate Filament Networks in Living Cells

1998 ◽  
Vol 143 (1) ◽  
pp. 147-157 ◽  
Author(s):  
Miri Yoon ◽  
Robert D. Moir ◽  
Veena Prahlad ◽  
Robert D. Goldman
Keyword(s):  
Intermediate Filament ◽  
Cell Shape ◽  
Fluorescence Recovery After Photobleaching ◽  
Fluorescent Protein ◽  
Time Lapse ◽  
Living Cells ◽  
A Cell ◽  
Filament Networks ◽  
Green Fluorescent ◽  
Vimentin Intermediate Filament

The motile properties of intermediate filament (IF) networks have been studied in living cells expressing vimentin tagged with green fluorescent protein (GFP-vimentin). In interphase and mitotic cells, GFP-vimentin is incorporated into the endogenous IF network, and accurately reports the behavior of IF. Time-lapse observations of interphase arrays of vimentin fibrils demonstrate that they are constantly changing their configurations in the absence of alterations in cell shape. Intersecting points of vimentin fibrils, or foci, frequently move towards or away from each other, indicating that the fibrils can lengthen or shorten. Fluorescence recovery after photobleaching shows that bleach zones across fibrils rapidly recover their fluorescence. During this recovery, bleached zones frequently move, indicating translocation of fibrils. Intriguingly, neighboring fibrils within a cell can exhibit different rates and directions of movement, and they often appear to extend or elongate into the peripheral regions of the cytoplasm. In these same regions, short filamentous structures are also seen actively translocating. All of these motile properties require energy, and the majority appear to be mediated by interactions of IF with microtubules and microfilaments.

scholarly journals Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks.

1993 ◽  
Vol 123 (3) ◽  
pp. 691-705 ◽  
Author(s):  
T S Stappenbeck ◽  
E A Bornslaeger ◽  
C M Corcoran ◽  
H H Luu ◽  
M L Virata ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Cultured Cells ◽  
Sequence Similarity ◽  
Full Length ◽  
Carboxyl Terminus ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Carboxyl Terminal ◽  
Filament Networks ◽  
Vimentin Intermediate Filament

We previously demonstrated that truncated desmoplakin I (DP I) molecules containing the carboxyl terminus specifically coalign with and disrupt both keratin and vimentin intermediate filament (IF) networks when overexpressed in tissue culture cells (Stappenbeck, T. S., and K. J. Green. J. Cell Biol. 116:1197-1209). These experiments suggested that the DP carboxyl-terminal domain is involved either directly or indirectly in linking IF with the desmosome. Using a similar approach, we have now investigated the behavior of ectopically expressed full-length DP I in cultured cells. In addition, we have further dissected the functional sequences in the carboxyl terminus of DP I that facilitate the interaction with IF networks. Transient transfection of a clone encoding full-length DP I into COS-7 cells produced protein that appeared in some cells to associate with desmosomes and in others to coalign with and disrupt IF. Deletion of the carboxyl terminus from this clone resulted in protein that still appeared capable of associating with desmosomes but not interacting with IF networks. As the amino terminus appeared to be dispensable for IF interaction, we made finer deletions in the carboxyl terminus of DP based on blocks of sequence similarity with the related molecules bullous pemphigoid antigen and plectin. We found a sequence at the very carboxyl terminus of DP that was necessary for coalignment with and disruption of keratin IF but not vimentin IF. Furthermore, the coalignment of specific DP proteins along keratin IF but not vimentin IF was correlated with resistance to extraction by Triton. The striking uncoupling resulting from the deletion of specific DP sequences suggests that the carboxyl terminus of DP interacts differentially with keratin and vimentin IF networks.

scholarly journals Mechanical Properties of Vimentin Intermediate Filament Networks

2014 ◽  
Vol 106 (2) ◽  
pp. 785a
Author(s):  
Huayin Wu ◽  
Mikkel Jensen ◽  
Ming Guo ◽  
David A. Weitz
Keyword(s):  
Mechanical Properties ◽  
Intermediate Filament ◽  
Filament Networks ◽  
Vimentin Intermediate Filament

Vimentin Intermediate Filament Formation: In Vitro Measurement and Mathematical Modeling of the Filament Length Distribution during Assembly†

Langmuir ◽  
2009 ◽  
Vol 25 (15) ◽  
pp. 8817-8823 ◽  
Author(s):  
Stéphanie Portet ◽  
Norbert Mücke ◽  
Robert Kirmse ◽  
Jörg Langowski ◽  
Michael Beil ◽  
...  
Keyword(s):  
Mathematical Modeling ◽  
Intermediate Filament ◽  
Length Distribution ◽  
Filament Length ◽  
Filament Formation ◽  
Vimentin Intermediate Filament

Paranemin and the organization of desmin filament networks

2001 ◽  
Vol 114 (6) ◽  
pp. 1079-1089 ◽  
Author(s):  
S.C. Schweitzer ◽  
M.W. Klymkowsky ◽  
R.M. Bellin ◽  
R.M. Robson ◽  
Y. Capetanaki ◽  
...  
Keyword(s):  
Cell Lines ◽  
Intermediate Filament ◽  
Transgene Expression ◽  
De Novo ◽  
Muscle Cells ◽  
The Other ◽  
Intermediate Filament Proteins ◽  
Mouse Fibroblasts ◽  
Filament Networks ◽  
Filament Network

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, in contrast, does not form extended filament networks in either SW13/cl.2 or intermediate filament-free mouse fibroblasts. Rather, desmin formed short thickened filamentous structures and prominent spot-like cytoplasmic aggregates that were composed of densely packed 9–11 nm diameter filaments. Analysis of stably transfected cell lines indicates that the inability of desmin to form extended networks is not due to a difference in the level of transgene expression. Nestin, paranemin and synemin are large intermediate filament proteins that coassemble with desmin in muscle cells. Although each of these large intermediate filament proteins colocalized with desmin when coexpressed in SW-13 cells, expression of paranemin, but not synemin or nestin, led to the formation of an extended desmin network. A similar rescue of desmin network organization was observed when desmin was coexpressed with vimentin, which coassembles with desmin, or with keratins, which formed a distinct filament network. These studies demonstrate that desmin filaments differ in their organizational properties from the other vimentin-like intermediate filament proteins and appear to depend upon coassembly with paranemin, at least when they are expressed in non-muscle cells, in order to form an extended filament network.

scholarly journals Properties of Intermediate Filament Networks Assembled from Keratin 8 and 18 in the Presence of Mg2+

2012 ◽  
Vol 103 (2) ◽  
pp. 195-201 ◽  
Author(s):  
Anke Leitner ◽  
Tobias Paust ◽  
Othmar Marti ◽  
Paul Walther ◽  
Harald Herrmann ◽  
...  
Keyword(s):  
Intermediate Filament ◽  
Keratin 8 ◽  
Filament Networks
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