First published online April 3, 2008
Journal of Cell Science 121, 804e (2008)
© The Company of Biologists Limited
Trephin takes up the yolk
During oogenesis in the mosquito, the ingestion of blood stimulates vitellogenesis – the uptake and storage of yolk by the oocyte. The yolk proteins vitellogenin and lipophorin are rapidly endocytosed via specific transmembrane receptors, both of which are members of the LDL-receptor superfamily. In mammals, such receptors are internalised by a clathrin-mediated route in which phosphotyrosine-binding (PTB) domain proteins such as ARH dock at the receptor's cytosolic FxNPxY motif, but it is not known whether a similar mechanism exists in the mosquito. On page 1264, Linton Traub and colleagues identify a mosquito protein, which they term trephin, that is orthologous to ARH. Similar to ARH, trephin binds to FxNPxY motifs, and also to clathrin and PtdIns[4,5]P2. Trephin also binds to the clathrin adaptor AP-2; however, unlike ARH and other mammalian PTB proteins (which bind to the
-platform subdomain), trephin binds to the β-platform subdomain of AP-2, indicating that a switch in domain specificity has occurred during evolution. Importantly, the expression of trephin is strongly upregulated in the oocyte following a blood meal, which is consistent with a role in the endocytosis of yolk proteins. These results elucidate a novel mechanism of clathrin-mediated endocytosis in the mosquito.

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