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EphA2 proteomics in human keratinocytes reveals a novel association with afadin and epidermal tight junctions.
Perez White, Bethany E; Ventrella, Rosa; Kaplan, Nihal; Cable, Calvin J; Thomas, Paul M; Getsios, Spiro.
Afiliação
  • Perez White BE; Department of Dermatology, Northwestern University, Chicago, IL 60611, USA.
  • Ventrella R; Department of Dermatology, Northwestern University, Chicago, IL 60611, USA.
  • Kaplan N; Department of Dermatology, Northwestern University, Chicago, IL 60611, USA.
  • Cable CJ; Department of Dermatology, Northwestern University, Chicago, IL 60611, USA.
  • Thomas PM; Proteomics Center of Excellence, Northwestern University, Chicago, IL 60611, USA.
  • Getsios S; Department of Molecular Biosciences, Northwestern University, Chicago, IL 60611, USA.
J Cell Sci ; 130(1): 111-118, 2017 01 01.
Article em En | MEDLINE | ID: mdl-27815408
ABSTRACT
EphA2 is a receptor tyrosine kinase that helps to maintain epidermal tissue homeostasis. A proximity-dependent biotin identification (BioID) approach was used to identify proteins in close proximity to EphA2 within primary human keratinocytes and three-dimensional (3D) reconstituted human epidermis (RHE) cultures to map a putative protein interaction network for this membrane receptor that exhibits a polarized distribution in stratified epithelia. Although a subset of known EphA2 interactors were identified in the BioID screen, >97% were uniquely detected in keratinocytes with over 50% of these vicinal proteins only present in 3D human epidermal culture. Afadin (AFDN), a cytoskeletal and junction-associated protein, was present in 2D and 3D keratinocyte cultures, and validated as a so-far-unknown EphA2-interacting protein. Loss of EphA2 protein disrupted the subcellular distribution of afadin and occludin in differentiated keratinocytes, leading to impairment of tight junctions. Collectively, these studies illustrate the use of the BioID approach in order to map receptor interaction networks in 3D human epithelial cultures, and reveal a positive regulatory role for EphA2 in the organization of afadin and epidermal tight junctions.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Queratinócitos / Junções Íntimas / Receptor EphA2 / Proteômica / Epiderme / Proteínas dos Microfilamentos Tipo de estudo: Prognostic_studies / Risk_factors_studies Limite: Humans / Male / Newborn Idioma: En Revista: J Cell Sci Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Queratinócitos / Junções Íntimas / Receptor EphA2 / Proteômica / Epiderme / Proteínas dos Microfilamentos Tipo de estudo: Prognostic_studies / Risk_factors_studies Limite: Humans / Male / Newborn Idioma: En Revista: J Cell Sci Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos