The fate of internalized α5 integrin is regulated by matrix-capable fibronectin
Hsia HC, Nair MR, Corbett SA. The fate of internalized α5 integrin is regulated by matrix-capable fibronectin. Journal Of Surgical Research 2014, 191: 268-279. PMID: 25062814, PMCID: PMC4160403, DOI: 10.1016/j.jss.2014.05.084.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCHO CellsCricetinaeCricetulusCytoplasmFibronectinsHumansIntegrin alpha5MiceMolecular Sequence DataProteasome Endopeptidase ComplexUbiquitinationConceptsFibronectin matrix assemblyΑ5 integrinFibronectin matrixMatrix assemblySpecific lysine residuesMouse embryo fibroblast cellsEmbryo fibroblast cellsExtracellular spaceIntegrin turnoverCytoplasmic tailTissue-remodeling processesAbsence of fibronectinInternalized receptorsLysine residuesReceptor turnoverIntegrinsTissue remodelingUbiquitinationProtein levelsChinese hamsterFibroblast cellsFibronectin dimersWound repairRapid degradationFate