Branching of keratin intermediate filaments

Nafeey, Soufi; Martin, Ines; Felder, Tatiana; Walther, Paul; Felder, Edward

doi:10.1016/j.jsb.2016.03.023

Cited by 14 publications

(9 citation statements)

References 33 publications

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“…A typical AFM image is shown in Fig. 3a and the filament heights agree with literature [2,30]. The average height for keratin IFs increases from LB to HB by a factor of 1.2 ± 0.4 and the height of vimentin IFs by a factor of 2.6 ± 0.9 (Fig.…”

supporting

confidence: 86%

Lateral Subunit Coupling Determines Intermediate Filament Mechanics

et al. 2019

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The cytoskeleton is a composite network of three types of protein filaments, among which intermediate filaments (IFs) are the most extensible ones. Two very important IFs are keratin and vimentin, which have similar molecular architectures, but different mechanical behaviors. Here we compare the mechanical response of single keratin and vimentin filaments using optical tweezers. We show that the mechanics of vimentin strongly depends on the ionic strength of the buffer and that its force-strain curve suggests a high degree of cooperativity between subunits. Indeed, a computational model indicates that in contrast to keratin, vimentin is characterized by strong lateral subunit coupling of its charged monomers during unfolding of α-helices. We conclude that cells can tune their mechanics by differential use of keratin versus vimentin.

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supporting

confidence: 86%

Lateral Subunit Coupling Determines Intermediate Filament Mechanics

et al. 2019

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“…However, these properties are conferred during posttranslational modifications, including phosphorylation and glycosylation (Lange et al, 2016), and also by some keratin-linked proteins (Bragulla and Homberger, 2009). Keratins also possess the tripartite structure uniformly shared among the IF proteins: "a highly conserved central α-helical rod domain flanked by a nonα-helical amino-terminal head domain and carboxy-terminal tail domain" (Nafeey et al, 2016). The unique pliable nature of IFs forms the basis for their role as a mechanical cushion that shields cells from external stressors (Leitner et al, 2012;Feroz et al, 2020).…”

Section: Structural Complexity Of Keratinmentioning

confidence: 99%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

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“…Strikingly, when both the keratin and vimentin intermediate filaments are expressed in a cell type they display distinct spatial organization of intermediate filament arrays (Osborn et al, 1980 ). Typically keratin intermediate filaments are packaged into bundles called tonofibrils (Steinert et al, 1981a ) and also form bifurcations (Nafeey et al, 2016 ). On the other hand, vimentin intermediate filaments are loosely arranged in a parallel or crisscross fashion forming a fine mesh network (Goldman et al, 1986 ).…”

Section: Cytoplasmic Intermediate Filaments-general Overviewmentioning

confidence: 99%

Intermediate Filaments at the Junction of Mechanotransduction, Migration, and Development

Sanghvi-Shah

Weber

2017

Front. Cell Dev. Biol.

132

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Mechanically induced signal transduction has an essential role in development. Cells actively transduce and respond to mechanical signals and their internal architecture must manage the associated forces while also being dynamically responsive. With unique assembly-disassembly dynamics and physical properties, cytoplasmic intermediate filaments play an important role in regulating cell shape and mechanical integrity. While this function has been recognized and appreciated for more than 30 years, continually emerging data also demonstrate important roles of intermediate filaments in cell signal transduction. In this review, with a particular focus on keratins and vimentin, the relationship between the physical state of intermediate filaments and their role in mechanotransduction signaling is illustrated through a survey of current literature. Association with adhesion receptors such as cadherins and integrins provides a critical interface through which intermediate filaments are exposed to forces from a cell's environment. As a consequence, these cytoskeletal networks are posttranslationally modified, remodeled and reorganized with direct impacts on local signal transduction events and cell migratory behaviors important to development. We propose that intermediate filaments provide an opportune platform for cells to both cope with mechanical forces and modulate signal transduction.

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Branching of keratin intermediate filaments

Cited by 14 publications

References 33 publications

Lateral Subunit Coupling Determines Intermediate Filament Mechanics

Lateral Subunit Coupling Determines Intermediate Filament Mechanics

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Intermediate Filaments at the Junction of Mechanotransduction, Migration, and Development

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