| First Author | Wu S | Year | 2016 |
| Journal | Proc Natl Acad Sci U S A | Volume | 113 |
| Issue | 35 | Pages | 9816-21 |
| PubMed ID | 27540116 | Mgi Jnum | J:235591 |
| Mgi Id | MGI:5796871 | Doi | 10.1073/pnas.1611189113 |
| Citation | Wu S, et al. (2016) Clathrin light chains' role in selective endocytosis influences antibody isotype switching. Proc Natl Acad Sci U S A 113(35):9816-21 |
| abstractText | 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 beta receptor 2 (TGFbetaR2) 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 delta-opioid receptor, but not the beta2-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. |
