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Clathrin light chains’ role in selective endocytosis influences antibody isotype switching.

Clathrin light chains’ role in selective endocytosis influences antibody isotype switching.
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Wu S, Majeed SR, Evans TM, Camus MD, Wong NM, Schollmeier Y, Park M, Muppidi JR, Reboldi A, Parham P, Cyster JG, Brodsky FM,


Wu S, Majeed SR, Evans TM, Camus MD, Wong NM, Schollmeier Y, Park M, Muppidi JR, Reboldi A, Parham P, Cyster JG, Brodsky FM, (click to view)

Wu S, Majeed SR, Evans TM, Camus MD, Wong NM, Schollmeier Y, Park M, Muppidi JR, Reboldi A, Parham P, Cyster JG, Brodsky FM,

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Proceedings of the National Academy of Sciences of the United States of America 2016 8 18() pii

Abstract

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 β receptor 2 (TGFβR2) 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 β2-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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