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First published online 16 June 2009
doi: 10.1242/jcs.041137

Journal of Cell Science 122, 2453-2463 (2009)
Published by The Company of Biologists 2009
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Research Article

The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway

Debarati Mukherjee1,*, Brian G. Coon1,*, Daniel F. Edwards, III1, Claudia B. Hanna1, Silvia A. Longhi2,{dagger}, J. Michael McCaffery3, Beverly Wendland3, Lilia A. Retegui2, Erfei Bi4 and R. Claudio Aguilar1,{ddagger}

1 Department of Biological Sciences, Purdue Cancer Center, Purdue University, West Lafayette, IN 47907, USA
2 Departamento de Química Biológica, Universidad de Buenos Aires, Buenos Aires, Argentina
3 Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA
4 Department of Cell and Developmental Biology, School of Medicine, University of Pennsylvania, Pennsylvania, PA 19104, USA

{ddagger} Author for correspondence (e-mail: Claudio{at}purdue.edu)

Accepted 15 April 2009

The epsins are a family of adaptors involved in recruiting other endocytic proteins, binding of ubiquitylated cargo and induction of membrane curvature. These molecules bear a characteristic epsin N-terminal homology (ENTH) domain and multiple peptide motifs that mediate protein-protein interactions. We have previously demonstrated that the ENTH domain of epsin is involved in Cdc42 signaling regulation. Here, we present evidence that yeast epsin 2 (Ent2) plays a signaling role during cell division. We observed that overexpression of the ENTH domain of Ent2 (ENTH2), but not Ent1, promoted the formation of chains of cells and aberrant septa. This dominant-negative effect resulted from ENTH2-mediated interference with septin assembly pathways. We mapped the ENTH2 determinants responsible for induction of the phenotype and found them to be important for efficient binding to the septin regulatory protein, Bem3. Supporting a physiological role for epsin 2 in cell division, the protein localized to sites of polarized growth and cytokinesis and rescued a defect in cell division induced by Bem3 misregulation. Collectively, our findings provide a potential molecular mechanism linking endocytosis (via epsin 2) with signaling pathways regulating cell division.

Key words: Cell division, Epsin, Septin, Endocytosis


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