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First published online April 3, 2008


Journal of Cell Science 121, 804e (2008)
© The Company of Biologists Limited
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In this issue

Trephin takes up the yolk


Figure 1

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 {alpha}-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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Related articles in JCS:

Internalization of LDL-receptor superfamily yolk-protein receptors during mosquito oogenesis involves transcriptional regulation of PTB-domain adaptors
Sanjay K. Mishra, Anupma Jha, Amie L. Steinhauser, Vladimir A. Kokoza, Charles H. Washabaugh, Alexander S. Raikhel, Woodbridge A. Foster, and Linton M. Traub
JCS 2008 121: 1264-1274. [Abstract] [Full Text]  




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