Diversity of Trichocyte Keratins and Keratin Associated Proteins

Plowman, Jeffrey E.

doi:10.1007/978-981-10-8195-8_3

Cited by 15 publications

(16 citation statements)

References 56 publications

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“…The high cysteine content of EDDM is comparable to that of avian EDCRP, another cysteine-rich protein component of feathers (Strasser et al 2015), and mammalian cysteine-rich keratin-associated proteins (KRTAPs), which are components of hair and nails (Rogers et al 2001; Deb-Choudhury 2018; Plowman 2018; Wu and Irwin 2018). While KRTAPs are encoded by genes outside of the EDC, the EDCRP gene is located in the EDC but within a different region than EDDM (Fig.…”

Section: Discussionmentioning

confidence: 99%

Immunolocalization and phylogenetic profiling of the feather protein with the highest cysteine content

et al. 2019

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Feathers are the most complex skin appendages of vertebrates. Mature feathers consist of interconnected dead keratinocytes that are filled with heavily cross-linked proteins. Although the molecular architecture determines essential functions of feathers, only few feather proteins have been characterized with regard to their amino acid sequences and evolution. Here, we identify Epidermal Differentiation protein containing DPCC Motifs (EDDM) as a cysteine-rich protein that has co-evolved with other feather proteins. The EDDM gene is located within the avian epidermal differentiation complex (EDC), a cluster of genes that has originated and diversified in amniotes. EDDM shares the exon-intron organization with EDC genes of other amniotes, including humans, and a gene encoding an EDDM-like protein is present in crocodilians, suggesting that avian EDDM arose by sequence modification of an epidermal differentiation gene present in a common ancestor of archosaurs. The EDDM protein contains multiple sequence repeats and a higher number of cysteine residues than any other protein encoded in the EDC. Immunohistochemical analysis of chicken skin and skin appendages showed expression of EDDM in barb and barbules of feathers as well as in the subperiderm on embryonic scutate scales. These results suggest that the diversification and differential expression of EDDM , besides other EDC genes, was instrumental in facilitating the evolution of the most complex molecular architecture of feathers. Electronic supplementary material The online version of this article (10.1007/s00709-019-01381-3) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Immunolocalization and phylogenetic profiling of the feather protein with the highest cysteine content

et al. 2019

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“…Otherwise, the interaction of the DNAbinding transcriptional repressor MOK2 with its lamin A/C-binding partner is prevented when MOK2 is phosphorylated at Ser38 and Ser129 by JNK3/JSAP1 [153]. Note that a large family of IFAPs, not reviewed in Supplementary Table S1, enclosed a hundred of KAPs (keratin-associated proteins) found in trichocyte cells, where they crosslink the keratin filaments in hair and wool fibers (for review [154]). Considering the importance of IFAPs in interlinking IFs to other cytoskeleton and cellular components, we speculate that some of these crosstalk proteins should be uncovered in the future as direct targets of JNKs.…”

Section: Phosphorylation Of If Proteins and Ifaps By Jnkmentioning

confidence: 99%

Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators

Benoit

Baillet

Poüs

2021

IJMS

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This review extensively reports data from the literature concerning the complex relationships between the stress-induced c-Jun N-terminal kinases (JNKs) and the four main cytoskeleton elements, which are actin filaments, microtubules, intermediate filaments, and septins. To a lesser extent, we also focused on the two membrane-associated cytoskeletons spectrin and ESCRT-III. We gather the mechanisms controlling cytoskeleton-associated JNK activation and the known cytoskeleton-related substrates directly phosphorylated by JNK. We also point out specific locations of the JNK upstream regulators at cytoskeletal components. We finally compile available techniques and tools that could allow a better characterization of the interplay between the different types of cytoskeleton filaments upon JNK-mediated stress and during development. This overview may bring new important information for applied medical research.

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“…Orthocortex and paracortex differ in macrofibril organization and protein composition, 3 and most notably in disulfide-bond rich KAPs. 30 Orthocortical cells have fewer species of high-disulfide KAPs and their macrofibrils have a helically twisted architecture, producing discrete columns which have circular profiles as visualized using transmission electron microscopy (Figure 2(a)). Paracortical cells contain a greater number of high-sulfur KAP species, the KIFs tend to be further apart, and helical twisting is of low intensity or absent.…”

Section: Mechanical Properties Of Fiber Componentsmentioning

confidence: 99%

A modular modeling approach for investigating wool critical buckling from biologically variable along-fiber microstructure

Vetharaniam

Plowman

Brorens

et al. 2020

Textile Research Journal

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Mammalian hair fibers are internally sophisticated. We introduce a modeling approach aimed at use in research that derives value from understanding how microstructural organization generates effects at the macroscopic level in the context of natural biological variation. Critical buckling load is solved using a numerical approach applied to a modular fiber microstructure model where fibers of arbitrary length are made up of snippets composed of serial cross-sections at 25 micrometer intervals. As an example, the model is applied to investigate how much effect changes to single microstructural properties (fiber ellipticity, cortical cell type distribution and cell type proportion) have on critical buckling load in the context of prickle. Potential uses and key weak areas in our knowledge of wool fiber morphology and biophysics are discussed.

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Diversity of Trichocyte Keratins and Keratin Associated Proteins

Cited by 15 publications

References 56 publications

Immunolocalization and phylogenetic profiling of the feather protein with the highest cysteine content

Immunolocalization and phylogenetic profiling of the feather protein with the highest cysteine content

Cytoskeleton and Associated Proteins: Pleiotropic JNK Substrates and Regulators

A modular modeling approach for investigating wool critical buckling from biologically variable along-fiber microstructure

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