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Vol. 19, Issue 7, 2936-2948, July 2008

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Interaction between Epsin/Yap180 Adaptors and the Scaffolds Ede1/Pan1 Is Required for Endocytosis

Lymarie Maldonado-Báez^*, Michael R. Dores, Edward M. Perkins, Theodore G. Drivas^*, Linda Hicke, and Beverly Wendland^*

*Department of Biology and Integrated Imaging Center, The Johns Hopkins University, Baltimore, MD 21218; and Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208

Submitted October 10, 2007; Revised April 16, 2008; Accepted April 22, 2008
Monitoring Editor: Howard Riezman

The spatial and temporal regulation of the interactions among the 60 proteins required for endocytosis is under active investigation in many laboratories. We have identified the interaction between monomeric clathrin adaptors and endocytic scaffold proteins as a critical prerequisite for the recruitment and/or spatiotemporal dynamics of endocytic proteins at early and late stages of internalization. Quadruple deletion yeast cells () lacking four putative adaptors, Ent1/2 and Yap1801/2 (homologues of epsin and AP180/CALM proteins), with a plasmid encoding Ent1 or Yap1802 mutants, have defects in endocytosis and growth at 37°C. Live-cell imaging revealed that the dynamics of the early- and late-acting scaffold proteins Ede1 and Pan1, respectively, depend upon adaptor interactions mediated by adaptor asparagine-proline-phenylalanine motifs binding to scaffold Eps15 homology domains. These results suggest that adaptor/scaffold interactions regulate transitions from early to late events and that clathrin adaptor/scaffold protein interaction is essential for clathrin-mediated endocytosis.

Address correspondence to: Beverly Wendland (bwendland{at}jhu.edu)

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