High impact information on EPPK1

• As reported previously this protein, which we call epiplakin, belongs to the plakin family, but it has some very unusual features [1].
• Epitope mapping experiments showed that the original patient's serum recognized a sequence unique to epiplakin, which was not found in plectin [1].
• Immunofluorescence staining revealed the presence of epiplakin in whole sheets of epidermis and esophagus, in glandular cells of eccrine sweat and parotid glands and in mucous epithelial cells in the stomach and colon [1].
• Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization [1].
• Epiplakin has 13 domains that are homologous to the B domain in the COOH-terminal region of desmoplakin [1].

Anatomical context of EPPK1

• We suggest that epiplakin is a cytolinker involved in maintaining the integrity of IF networks in simple epithelial cells [2].
• Furthermore, we observed an increase of epiplakin expression in keratinocytes after the calcium switch, suggesting the involvement of epiplakin in the process of keratinocyte differentiation [2].
• Interactions between epiplakin and intermediate filaments [3].

Physical interactions of EPPK1

• At least two of the 4.6 copies in the B domains of epiplakin were necessary for the binding of fusion proteins to keratin [3].

Other interactions of EPPK1

• The repeated structures of linker domains also played an important role in the binding of epiplakin to keratin in these assays while also increasing the repeated structure in the linker domain of epiplakin which is involved in the increased binding to IF [3].

References