{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Roberts BJ"],"funding":["NIGMS NIH HHS"],"pagination":["e77012"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3790753"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(10)"],"pubmed_abstract":["Desmosomes are prominent cell-cell adhesive junctions in stratified squamous epithelia and disruption of desmosomal adhesion has been shown to have dramatic effects on the function and integrity of these tissues. During normal physiologic processes, such as tissue development and wound healing, intercellular adhesion must be modified locally to allow coordinated cell movements. The mechanisms that control junction integrity and adhesive strength under these conditions are poorly understood. We utilized a proteomics approach to identify plakophilin-3 associated proteins and identified the 14-3-3 family member stratifin. Stratifin interacts specifically with plakophilin-3 and not with other plakophilin isoforms and mutation analysis demonstrated the binding site includes serine 285 in the am"],"journal":["PloS one"],"pubmed_title":["Stratifin (14-3-3 σ) limits plakophilin-3 exchange with the desmosomal plaque."],"pmcid":["PMC3790753"],"funding_grant_id":["P20GM103489","P20 GM103489"],"pubmed_authors":["Reddy R","Wahl JK","Roberts BJ"],"additional_accession":[]},"is_claimable":false,"name":"Stratifin (14-3-3 σ) limits plakophilin-3 exchange with the desmosomal plaque.","description":"Desmosomes are prominent cell-cell adhesive junctions in stratified squamous epithelia and disruption of desmosomal adhesion has been shown to have dramatic effects on the function and integrity of these tissues. During normal physiologic processes, such as tissue development and wound healing, intercellular adhesion must be modified locally to allow coordinated cell movements. The mechanisms that control junction integrity and adhesive strength under these conditions are poorly understood. We utilized a proteomics approach to identify plakophilin-3 associated proteins and identified the 14-3-3 family member stratifin. Stratifin interacts specifically with plakophilin-3 and not with other plakophilin isoforms and mutation analysis demonstrated the binding site includes serine 285 in the am","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013","modification":"2026-04-20T03:12:22.641Z","creation":"2019-03-26T23:16:28Z"},"accession":"S-EPMC3790753","cross_references":{"pubmed":["24124604"],"doi":["10.1371/journal.pone.0077012"]}}