Differential nucleocytoplasmic trafficking between the related endocytic proteins Eps15 and Eps15R

Viviane Poupon, Simona Polo, Manuela Vecchi, Gwendal Martin, Alice Dautry-Varsat, Nadine Cerf-Bensussan, Pier Paolo Di Fiore, Alexandre Benmerah

Research output: Contribution to journalArticlepeer-review

Abstract

Eps15 and Eps15R are constitutive components of clathrin-coated pits that are required for clathrin-dependent endocytosis. The most striking difference between these two related proteins is that Eps15R is also found in the nucleus, whereas Eps15 is excluded from this compartment at steady state. To better understand the individual functions of these two proteins, the mechanisms responsible for their different localization were investigated. Interestingly, some mutants of Eps15 were found in the nucleus. This nuclear localization was correlated with the loss of the last ∼100 amino acids of Eps15, suggesting the presence of a nuclear export signal (NES) within this region. As expected, the last 25 amino acids contain a leucine-rich sequence matching with classical NESs, show a leptomycin B-sensitive nuclear export activity, and bind to the exportin CRM1 in a leucine residue-dependent manner. In contrast, no NES could be found in Eps15R, a result in keeping with its constitutive nuclear localization that appears to be regulated by alternative splicing. Altogether, these results are the first characterization of nucleocytoplasmic shuttling signals for endocytic proteins. They also provide an explanation for the different nuclear localization of Eps15 and Eps15R and further evidence for a possible nuclear function for Eps15 protein family members.

Original languageEnglish
Pages (from-to)8941-8948
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number11
DOIs
Publication statusPublished - Mar 15 2002

ASJC Scopus subject areas

  • Biochemistry

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