AI Article Synopsis
- Clathrin-mediated endocytosis happens at various sites on the cell membrane, but the selection of these sites and recognition of different cargo remains unclear.
- FCHO1 and FCHO2 proteins are early participants at clathrin sites and might play a crucial role in setting up the necessary structures, but their exact influence compared to another protein, AP-2, is being questioned.
- Research shows that FCHO1 interacts with the Bmp receptor in zebrafish, suggesting it helps enhance Bmp signaling; however, its role is different from that of AP-2, indicating a more complex mechanism in clathrin coat assembly.
Article Abstract
Clathrin-mediated endocytosis occurs at multiple independent import sites on the plasma membrane, but how these positions are selected and how different cargo is simultaneously recognized is obscure. FCHO1 and FCHO2 are early-arriving proteins at surface clathrin assemblies and are speculated to act as compulsory coat nucleators, preceding the core clathrin adaptor AP-2. Here, we show that the μ-homology domain of FCHO1/2 represents an endocytic interaction hub. Translational silencing of fcho1 in zebrafish embryos causes strong dorsoventral patterning defects analogous to Bmp signal failure. The Fcho1 μ-homology domain interacts with the Bmp receptor Alk8, uncovering an endocytic component that positively modulates Bmp signal transmission. Still, the fcho1 morphant phenotype is distinct from severe embryonic defects apparent when AP-2 is depleted. Our data thus challenge the primacy of FCHO1/2 in coat initiation.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3354769 | PMC |
| http://dx.doi.org/10.1038/ncb2473 | DOI Listing |
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