The Small Heat Shock Protein Hsp27 Affects Assembly Dynamics and Structure of Keratin Intermediate Filament Networks

Kayser, Jona; Haslbeck, Martin; Dempfle, L.; Krause, Maike; Grashoff, Carsten; Büchner, Johannes; Herrmann, Harald; Bausch, Andreas R.

doi:10.1016/j.bpj.2013.09.007

Cited by 48 publications

(43 citation statements)

References 43 publications

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“…In addition to posttranslational modifications, the small heat shock protein Hsp27 and proteins of the plakin and S100 families regulate keratin assembly, bundling, and network organization (Windoffer et al 2011;Kayser et al 2013;Bouameur et al 2014;Lesniak and Graczyk-Jarzynka 2015). Plectin is a plakin protein that links keratin bundling to MAPK signaling.…”

Section: Intrinsic Keratin Properties and Associated Proteins As Detementioning

confidence: 99%

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

Hatzfeld

Keil

Magin

2017

Cold Spring Harb Perspect Biol

114

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Adherens junctions (AJs) and desmosomes connect the actin and keratin filament networks of adjacent cells into a mechanical unit. Whereas AJs function in mechanosensing and in transducing mechanical forces between the plasma membrane and the actomyosin cytoskeleton, desmosomes and intermediate filaments (IFs) provide mechanical stability required to maintain tissue architecture and integrity when the tissues are exposed to mechanical stress. Desmosomes are essential for stable intercellular cohesion, whereas keratins determine cell mechanics but are not involved in generating tension. Here, we summarize the current knowledge of the role of IFs and desmosomes in tissue mechanics and discuss whether the desmosome-keratin scaffold might be actively involved in mechanosensing and in the conversion of chemical signals into mechanical strength.

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Section: Intrinsic Keratin Properties and Associated Proteins As Detementioning

confidence: 99%

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

Hatzfeld

Keil

Magin

2017

Cold Spring Harb Perspect Biol

114

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“…The association of IF with small heat-shock proteins (sHSPs) and other chaperones was observed in a variety of cells expressing different types of IFs (40)(41)(42)(43)(44). A role for this interaction during IF assembly has been suggested because sHSPs were shown to influence IF solubility (42).…”

Section: Controlmentioning

confidence: 99%

Vimentin filament precursors exchange subunits in an ATP-dependent manner

Ahrends

Rossow

Hookway

et al. 2015

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

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Intermediate filaments (IFs) are a component of the cytoskeleton capable of profound reorganization in response to specific physiological situations, such as differentiation, cell division, and motility. Various mechanisms were proposed to be responsible for this plasticity depending on the type of IF polymer and the biological context. For example, recent studies suggest that mature vimentin IFs (VIFs) undergo rearrangement by severing and reannealing, but direct subunit exchange within the filament plays little role in filament dynamics at steady state. Here, we studied the dynamics of subunit exchange in VIF precursors, called unit-length filaments (ULFs), formed by the lateral association of eight vimentin tetramers. To block vimentin assembly at the ULF stage, we used the Y117L vimentin mutant (vimentin Y117L ). By tagging vimentin Y117L with a photoconvertible protein mEos3.2 and photoconverting ULFs in a limited area of the cytoplasm, we found that ULFs, unlike mature filaments, were highly dynamic. Subunit exchange among ULFs occurred within seconds and was limited by the diffusion of soluble subunits in the cytoplasm rather than by the association and dissociation of subunits from ULFs. Our data demonstrate that cells expressing vimentin Y117L contained a large pool of soluble vimentin tetramers that was in rapid equilibrium with ULFs. Furthermore, vimentin exchange in ULFs required ATP, and ATP depletion caused a dramatic reduction of the soluble tetramer pool. We believe that the dynamic exchange of subunits plays a role in the regulation of ULF assembly and the maintenance of a soluble vimentin pool during the reorganization of filament networks.ell shape, mechanical properties, and motile behavior are determined by the cytoskeleton composed of three interconnected polymers: actin microfilaments, microtubules, and intermediates filaments (IFs). Whereas the structural polarity of microfilaments and microtubules is essential for their functions, IFs are apolar structures that contribute to the mechanical properties of the cell (reviewed in ref.

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“…For instance, HspB5 (αB-crystallin) interacts and affects assembly and selfassociation of desmin (Houck et al 2011;Ghosh et al 2007;Perng et al 2004;Elliott et al 2013), GFAP (Ghosh et al 2007;Perng et al 1999), vimentin and peripherin (Djabali et al 1997), and keratin (Elliott et al 2013). HspB1 interacts with glial fibrillary acidic protein (Perng et al 1999), desmin (Perng et al 1999;Elliott et al 2013), and keratin (Kayser et al 2013). The data of cell biology (Evgrafov et al 2004;Ackerley et al 2006;Holmgren et al 2013) indicate that point mutants of HspB1 associated with distal hereditary motor neuropathy (or Charcot-Marie-Tooth disease) can affect the structure and intracellular transportation of neurofilaments.…”

Section: Discussionmentioning

confidence: 99%

“…HspB1 interacts with desmin less effectively than αB-crystallin; however, at high concentrations, it also prevents self-association of desmin filaments (Elliott et al 2013). HspB1 prevents keratin filament bundling and affects the assembly dynamics of intermediate filaments formed by keratin (Kayser et al 2013). Cotransfection of NFL and S135F mutant (but not the wild type) HspB1 results in altered neurofilament assembly in cells devoid of cytoplasmic intermediate filaments (Evgrafov et al 2004), whereas transient expression of P182L mutant of HspB1 in cortical cells is accompanied by disruption of neurofilament assembly and accumulation of aggregates containing NFM (Ackerley et al 2006).…”

Section: Introductionmentioning

confidence: 99%

Interaction of small heat shock proteins with light component of neurofilaments (NFL)

Nefedova

Sudnitsyna

Gusev

2017

Cell Stress and Chaperones

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The interaction of human small heat shock protein HspB1, its point mutants associated with distal hereditary motor neuropathy, and three other small heat shock proteins (HspB5, HspB6, HspB8) with the light component of neurofilaments (NFL) was analyzed by differential centrifugation, analytical ultracentrifugation, and fluorescent spectroscopy. The wild-type HspB1 decreased the quantity of NFL in pellets obtained after low-and high-speed centrifugation and increased the quantity of NFL remaining in the supernatant after high-speed centrifugation. Part of HspB1 was detected in the pellet of NFL after high-speed centrifugation, and at saturation, 1 mol of HspB1 monomer was bound per 2 mol of NFL. Point mutants of HspB1 associated with distal hereditary motor neuropathy (G84R, L99M, R140G, K141Q, and P182S) were almost as effective as the wild-type HspB1 in modulation of NFL assembly. At low ionic strength, HspB1 weakly interacted with NFL tetramers, and this interaction was increased upon salt-induced polymerization of NFL. HspB1 and HspB5 (αB-crystallin) decreased the rate of NFL polymerization measured by fluorescent spectroscopy. HspB6 (Hsp20) and HspB8 (Hsp22) were less effective than HspB1 (or HspB5) in modulation of NFL assembly. The data presented indicate that the small heat shock proteins affect NFL transition from tetramers to filaments, hydrodynamic properties of filaments, and their bundling and therefore probably modulate the formation of intermediate filament networks in neurons.

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The Small Heat Shock Protein Hsp27 Affects Assembly Dynamics and Structure of Keratin Intermediate Filament Networks

Cited by 48 publications

References 43 publications

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

Desmosomes and Intermediate Filaments: Their Consequences for Tissue Mechanics

Vimentin filament precursors exchange subunits in an ATP-dependent manner

Interaction of small heat shock proteins with light component of neurofilaments (NFL)

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