Identification of the C-Terminal Tail Domain of AHF/Trichohyalin as the Critical Site for Modulation of the Keratin Filamentous Meshwork in the Keratinocyte

The study identified the C-terminal tail domain of AHF/trichohyalin as crucial for modulating the keratin filamentous meshwork in keratinocytes. By introducing full-length and mutant AHF into keratinocyte cell lines, researchers observed that the full-length AHF formed small granules that bound to keratin filaments, affecting cell growth, mobility, and shape. Removing 6 amino acids from the C-terminal tail resulted in a loss of keratin adherence and enlarged granules. The findings suggested that AHF's C-terminus latches onto keratin bundles, rearranging the keratin meshwork through its cohesive activity, providing insights into cytoskeletal modulation in hair follicles.