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MBC in Press, published online ahead of print April 30, 2008
Mol. Biol. Cell 10.1091/mbc.E07-10-1019

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Submitted on October 10, 2007
Revised on April 16, 2008
Accepted on April 22, 2008

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

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

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

Monitoring Editor: Howard Riezman

The spatial and temporal regulation of the interactions among the ~60 proteins required for endocytosis are under active investigation in many labs. 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 ({Delta}{Delta}{Delta}{Delta}) 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 NPF motifs binding to scaffold EH 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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