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p97/VCP Promotes the Recycling of Endocytic Cargo.
Kawan, Mona; Körner, Maria; Schlosser, Andreas; Buchberger, Alexander.
Afiliação
  • Kawan M; Chair of Biochemistry I, University of Würzburg, Biocenter, Am Hubland, 97074 Würzburg, Germany.
  • Körner M; Chair of Biochemistry I, University of Würzburg, Biocenter, Am Hubland, 97074 Würzburg, Germany.
  • Schlosser A; Rudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Josef-Schneider-Straße 2, 97080 Würzburg, Germany.
  • Buchberger A; Chair of Biochemistry I, University of Würzburg, Biocenter, Am Hubland, 97074 Würzburg, Germany.
Mol Biol Cell ; 34(13): ar126, 2023 Dec 01.
Article em En | MEDLINE | ID: mdl-37756124
ABSTRACT
The endocytic pathway is of central importance for eukaryotic cells, as it enables uptake of extracellular materials, membrane protein quality control and recycling, as well as modulation of receptor signaling. While the ATPase p97 (VCP, Cdc48) has been found to be involved in the fusion of early endosomes and endolysosomal degradation, its role in endocytic trafficking is still incompletely characterized. Here, we identify myoferlin (MYOF), a ferlin family member with functions in membrane trafficking and repair, as a hitherto unknown p97 interactor. The interaction of MYOF with p97 depends on the cofactor PLAA previously linked to endosomal sorting. Besides PLAA, shared interactors of p97 and MYOF comprise several proteins involved in endosomal recycling pathways, including Rab11, Rab14, and the transferrin receptor CD71. Accordingly, a fraction of p97 and PLAA localizes to MYOF-, Rab11-, and Rab14-positive endosomal compartments. Pharmacological inhibition of p97 delays transferrin recycling, indicating that p97 promotes not only the lysosomal degradation, but also the recycling of endocytic cargo.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Endossomos / Proteínas de Membrana Limite: Humans Idioma: En Revista: Mol Biol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Endossomos / Proteínas de Membrana Limite: Humans Idioma: En Revista: Mol Biol Cell Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Alemanha
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