Cytoskeletal linker protein that connects to intermediate filaments and controls their reorganization in response to stress (PubMed:16382146, PubMed:20926261, PubMed:18285451, PubMed:25232867, PubMed:25617501, PubMed:23599337). In response to mechanical stress like wound healing, is associated with the machinery for cellular motility by slowing down keratinocyte migration and proliferation and accelerating keratin bundling in proliferating keratinocytes thus contributing to tissue architecture (PubMed:16382146, PubMed:20926261). However in wound healing in corneal epithelium also positively regulates cell differentiation and proliferation and negatively regulates migration thereby controlling corneal epithelium morphogenesis and integrity (PubMed:23599337). In response to cellular stress, plays a role in keratin filament reorganization, probably by protecting keratin filaments against disruption (PubMed:18285451). During liver and pancreas injuries, plays a protective role by chaperoning disease-induced intermediate filament reorganization (PubMed:25232867, PubMed:25617501). Interacts with KRT5, KRT14 and KRT5/KRT14 heterotetramer; interacts preferentially with assembled filaments rather than keratin monomers (PubMed:18285451). Interacts with KRT8 and KRT18 and KRT8/KRT18 heterotetramer; interacts preferentially with assembled filaments rather than keratin monomers (PubMed:25617501). Interacts with KRT1, VIM and DES; interaction is stronger with KRT1 than with VIM or DES; interaction is dependent of higher-order structure of intermediate filament (By similarity). Apicolateral cell membrane localization is keratin filaments-dependent (PubMed:25232867). May move dynamically from bundling intermediate filaments in the cytoplasm or at the cell periphery and reinforcing them. Decorates the keratin intermediate filaments (IF) network and partially that of vimentin (By similarity). High levels in skin, small intestine and salivary gland. Lower levels in lung, uterus and liver. Not detected in brain, kidney, muscle, heart or spleen. In skin, expressed in all epidermal layers but not in the dermis. In intestine, expressed exclusively in the epithelial cell layer of the villi. In liver, expressed at hepatocyte margins. Around the region of the wound, expressed in the upper half of the epidermis. Weakly expressed on the basilar side of the suprabasal layer of the epidermis at the wound's edge. Expressed strongly in the upper layer of the epidermis, especially in larger keratinocytes (PubMed:16382146). Expressed in undifferentiated primary keratinocytes (PubMed:18285451). Strongly expressed in ductal cells, and also expressed in acinar cells (PubMed:25232867). Expressed in hepatocytes and cholangiocytes (PubMed:25617501). Up-regulated upon calcium-mediated keratinocyte differentiation (PubMed:18285451). Up-regulated in hepatocytes during liver stress (PubMed:25617501). Plectin repeats are important for the binding to keratin and VIM and controls intermediate filament networks organization. Homozygous knockout mice develop normally and are healthy and fertile. Skin of homozygous knockout mice reveal no blistering and fragility. Exhibit slightly enhanced wound closure. Belongs to the plakin or cytolinker family.