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Clathrin light chains' role in selective endocytosis influences antibody isotype switching.
Wu, Shuang; Majeed, Sophia R; Evans, Timothy M; Camus, Marine D; Wong, Nicole M L; Schollmeier, Yvette; Park, Minjong; Muppidi, Jagan R; Reboldi, Andrea; Parham, Peter; Cyster, Jason G; Brodsky, Frances M.
Afiliação
  • Wu S; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Majeed SR; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Evans TM; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Camus MD; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Wong NM; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Schollmeier Y; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Park M; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
  • Muppidi JR; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143;
  • Reboldi A; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143;
  • Parham P; Department of Structural Biology, Stanford University, Stanford, CA 94305; Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305.
  • Cyster JG; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; f.brodsky@ucl.ac.uk jason.cyster@ucsf.edu.
  • Brodsky FM; Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94143; Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; Department of Microbiology and Immunology, University of California, San Francisco, CA 94143; The G. W.
Proc Natl Acad Sci U S A ; 113(35): 9816-21, 2016 08 30.
Article em En | MEDLINE | ID: mdl-27540116
Clathrin, a cytosolic protein composed of heavy and light chain subunits, assembles into a vesicle coat, controlling receptor-mediated endocytosis. To establish clathrin light chain (CLC) function in vivo, we engineered mice lacking CLCa, the major CLC isoform in B lymphocytes, generating animals with CLC-deficient B cells. In CLCa-null mice, the germinal centers have fewer B cells, and they are enriched for IgA-producing cells. This enhanced switch to IgA production in the absence of CLCa was attributable to increased transforming growth factor ß receptor 2 (TGFßR2) signaling resulting from defective endocytosis. Internalization of C-X-C chemokine receptor 4 (CXCR4), but not CXCR5, was affected in CLCa-null B cells, and CLC depletion from cell lines affected endocytosis of the δ-opioid receptor, but not the ß2-adrenergic receptor, defining a role for CLCs in the uptake of a subset of signaling receptors. This instance of clathrin subunit deletion in vertebrates demonstrates that CLCs contribute to clathrin's role in vivo by influencing cargo selectivity, a function previously assigned exclusively to adaptor molecules.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Linfócitos B / Deleção de Genes / Switching de Imunoglobulina / Cadeias Leves de Clatrina / Endocitose Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2016 Tipo de documento: Article País de publicação: Estados Unidos
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Linfócitos B / Deleção de Genes / Switching de Imunoglobulina / Cadeias Leves de Clatrina / Endocitose Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2016 Tipo de documento: Article País de publicação: Estados Unidos