Cell Biology

Endocytosis and the Nucleus

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Science  19 May 2000:
Vol. 288, Issue 5469, pp. 1139
DOI: 10.1126/science.288.5469.1139a

The protein epsin is known to bind to components of the clathrin coat that surrounds portions of the plasma membrane destined to be pinched off during endocytosis. The central and C-terminal domains of epsin contain the clathrin and clathrin adaptor binding sites, while the N-terminal domain had been shown to have an essential, albeit unknown, function on the basis of genetic studies. Hyman et al. find that the structure of the epsin N-terminal domain is similar to portions of proteins that are translocated from the cytoplasm to the nucleus. Following up this clue, they went on to demonstrate an interaction between epsin and a transcription factor, and observed regulated import of epsin into the nucleus. Thus, epsin may serve to convey signals from the endocytic pathway to the transcription machinery.—SMH

J. Cell Biol.149, 537 (2000).

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