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© The Rockefeller University Press, 0021-9525/2001//1511 $5.00
The Journal of Cell Biology, Volume 153, Number 7, , 2001 1511-1518

Nucleocytoplasmic Shuttling of Endocytic Proteins

^a Department of Experimental Oncology, European Institute of Oncology, 20141 Milan, Italy
^b Institut National de la Santé et de la Recherche Medicalé E9925, Faculté Necker-Enfants Malades, 75730 Paris, France
^c Institut de Formation aux Metiers Paramedicaux, Fondazione Italiana per la Ricerca sul Cancro, Institute for Molecular Oncology, 20139 Milan, Italy
^d Dipartimento di Medicina Chirurgia ed Odontoiatria, Universitá degli Studi di Milano, 20122 Milan, Italy
Istituto Europeo di Oncologia, Via Ripamonti 435, 20141 Milan, Italy.39-02-574-89-85139-02-574-89-855

pdifiore{at}ieo.it

Many cellular processes rely on the ordered assembly of macromolecular structures. Here, we uncover an unexpected link between two such processes, endocytosis and transcription. Many endocytic proteins, including eps15, epsin1, the clathrin assembly lymphoid myeloid leukemia (CALM), and -adaptin, accumulate in the nucleus when nuclear export is inhibited. Endocytosis and nucleocytoplasmic shuttling of endocytic proteins are apparently independent processes, since inhibition of endocytosis did not appreciably alter nuclear translocation of endocytic proteins, and blockade of nuclear export did not change the initial rate of endocytosis. In the nucleus, eps15 and CALM acted as positive modulators of transcription in a GAL4-based transactivation assay, thus raising the intriguing possibility that some endocytic proteins play a direct or indirect role in transcriptional regulation.

Key Words: endocytosis • nucleocytoplasmic shuttling • eps15 • CRM1 • transcription

© 2001 The Rockefeller University Press

Abbreviations used in this paper: CALM, clathrin assembly lymphoid myeloid leukemia; CRM, chromosomal region maintenance; EH, eps15 homology; LMB, leptomycin B; NES, nuclear export signal; Tf, transferrin.

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