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J. Biol. Chem., Vol. 278, Issue 4, 2686-2691, January 24, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/4/2686    most recent M201521200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Luque, C. M. Articles by Correas, I. Search for Related Content PubMed PubMed Citation Articles by Luque, C. M. Articles by Correas, I. Social Bookmarking                      What's this?

An Alternative Domain Containing a Leucine-rich Sequence Regulates Nuclear Cytoplasmic Localization of Protein 4.1R^*

Carlos M. Luque^§, Carmen M. Pérez-Ferreiro^¶, Alicia Pérez-González, Ludwig Englmeier^**, Maria D. Koffa, and Isabel Correas

From the  Departamento de Biología Molecular, Centro de Biología Molecular "Severo Ochoa" (Consejo Superior de Investigaciones Científicas/Universidad Autónoma de Madrid), Universidad Autónoma de Madrid, E-28049 Madrid, Spain and the  European Molecular Biology Laboratory, Gene Expression Programme, D-69117 Heidelberg, Germany

In red blood cells, protein 4.1 (4.1R) is an 80-kDa protein that stabilizes the spectrin-actin network and anchors it to the plasma membrane. The picture is more complex in nucleated cells, in which many 4.1R isoforms, varying in size and intracellular location, have been identified. To contribute to the characterization of signals involved in differential intracellular localization of 4.1R, we have analyzed the role the exon 5-encoded sequence plays in 4.1R distribution. We show that exon 5 encodes a leucine-rich sequence that shares key features with nuclear export signals (NESs). This sequence adopts the topology employed for NESs of other proteins and conserves two hydrophobic residues that are shown to be critical for NES function. A 4.1R isoform expressing the leucine-rich sequence binds to the export receptor CRM1 in a RanGTP-dependent fashion, whereas this does not occur in a mutant whose two conserved hydrophobic residues are substituted. These two residues are also essential for 4.1R intracellular distribution, because the 4.1R protein containing the leucine-rich sequence localizes in the cytoplasm, whereas the mutant protein predominantly accumulates in the nucleus. We hypothesize that the leucine-rich sequence in 4.1R controls distribution and concomitantly function of a specific set of 4.1R isoforms.

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