2012
DOI: 10.1016/j.jdermsci.2011.12.014
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Identification of the C-terminal tail domain of AHF/trichohyalin as the critical site for modulation of the keratin filamentous meshwork in the keratinocyte

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Cited by 12 publications
(14 citation statements)
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“…Genes located between the SFTP genes and S100A11 in X. laevis do not have homologs at syntenic positions in the genomes of amniotes ( Figure 1A). Of note, peptidoglycan recognition protein genes and loricrin-like genes, which are present in the epidermal differentiation complex (EDC) regions of humans and other amniotes, [17] are absent in the vicinity of frog SFTP genes.…”
Section: Resultsmentioning
confidence: 99%
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“…Genes located between the SFTP genes and S100A11 in X. laevis do not have homologs at syntenic positions in the genomes of amniotes ( Figure 1A). Of note, peptidoglycan recognition protein genes and loricrin-like genes, which are present in the epidermal differentiation complex (EDC) regions of humans and other amniotes, [17] are absent in the vicinity of frog SFTP genes.…”
Section: Resultsmentioning
confidence: 99%
“…The latter sequence motif (core sequence: SPLy(E/D)y) has been implicated in the interaction of SFTPs with keratin filaments. [14,17,23] The identification of sequence elements, such as the S100 domain and the carboxy-terminal motif, that are conserved in SFTPs of phylogenetically most diverse tetrapods indicates that these features were already present in evolutionarily ancient SFTPs and may help to define the functions of SFTP domains in future experimental studies.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…‘//’ indicates sequence gaps that were introduced to facilitate the depiction of all sequence ends. The sequence motif of trichohyalin that was investigated by Takase and Hirai ( 41 ) is underlined. The consensus sequence of the ancestral carboxy-terminal motif of SFTPs is shown below the alignment.…”
Section: Resultsmentioning
confidence: 99%
“…Recently, the C-terminal 13 amino acid sequence in the tail domain 9, which is conserved among species, was shown to be essential for keratin adherent ability of mouse TCHH in keratinocyte cell lines, though neither deimination nor isopeptide cross-links within the functionally critical sites has yet been determined. Based on these observations, Takase and Hirai ( 2012 ) proposed a principal role of the C-terminal tail domain of TCHH in adhesion to keratins. Following aggregation of N-terminal parts (i.e., N-terminal S100-like domain and following repetitive peptide domains) in TCHH, KIFs bundle and form meshes.…”
Section: Cit-tchh Susceptibility To Transglutaminasementioning
confidence: 99%