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MBC in Press, published online ahead of print May 23, 2007
Mol. Biol. Cell 10.1091/mbc.E07-05-0436

A more recent version of this article appeared on August 1, 2007
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Submitted on May 11, 2007
Accepted on May 11, 2007

Interaction of the Endocytic Scaffold Protein Pan1 with the Type I Myosins Contributes to the Late Stages of Endocytosis

Sarah L. Barker,*{dagger} Linda Lee,{ddagger} B. Daniel Pierce,* Lymarie Maldonado-Báez,* David G. Drubin,{ddagger} and Beverly Wendland*

*Department of Biology, The Johns Hopkins University, Baltimore, MD 21218; {ddagger}Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720

Monitoring Editor: Sandra Schmid

The yeast endocytic scaffold Pan1 contains an uncharacterized proline-rich domain (PRD) at its carboxy(C)-terminus. We report that the pan1-20 temperature sensitive allele has a disrupted PRD due to a frame-shift mutation in the open reading frame of the domain. To reveal redundantly masked functions of the PRD, a synthetic genetic array screens with a pan1{Delta}PRD strain found genetic interactions with alleles of ACT1, LAS17 and a deletion of SLA1. Through a yeast two hybrid screen, the SH3 domains of the type I myosins, Myo3 and Myo5, were identified as binding partners for the C-terminus of Pan1. In vitro and in vivo assays validated this interaction. The relative timing of recruitment of Pan1-GFP and Myo3/5-RFP at nascent endocytic sites was revealed by two-color real-time fluorescence microscopy; the type I myosins join Pan1 at cortical patches at a late stage of internalization, preceding the inward movement of Pan1 and its disassembly. In cells lacking the Pan1PRD we observed an increased lifetime of Myo5-GFP at the cortex. Finally, Pan1PRD enhanced the actin polymerization activity of Myo5-Vrp1 complexes using in vitro assays. We propose that Pan1 and the type I myosins interactions promote an actin activity important at a late stage in endocytic internalization.

{dagger}Present address: Banting and Best Department of Medical Research, Terence Donnelly Centre for Cellular and Biomolecular Research, 160 College Street, Toronto, ON, M5S 3E1 Canada.

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




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L. Maldonado-Baez, M. R. Dores, E. M. Perkins, T. G. Drivas, L. Hicke, and B. Wendland
Interaction between Epsin/Yap180 Adaptors and the Scaffolds Ede1/Pan1 Is Required for Endocytosis
Mol. Biol. Cell, July 1, 2008; 19(7): 2936 - 2948.
[Abstract] [Full Text] [PDF]


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