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Eps15 Homology Domain 1-associated Tubules Contain Phosphatidylinositol-4-Phosphate and Phosphatidylinositol-(4,5)-Bisphosphate and Are Required for Efficient Recycling

Jović, Marko, Kieken, Fabien, Naslavsky, Naava, Sorgen, Paul L., Caplan, Steve·2009·Molecular Biology of the Cell
DOI 10.1091/mbc.e08-11-1102
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Abstract

The C-terminal Eps15 homology domain (EHD) 1/receptor-mediated endocytosis-1 protein regulates recycling of proteins and lipids from the recycling compartment to the plasma membrane. Recent studies have provided insight into the mode by which EHD1-associated tubular membranes are generated and the mechanisms by which EHD1 functions. Despite these advances, the physiological function of these striking EHD1-associated tubular membranes remains unknown. Nuclear magnetic resonance spectroscopy demonstrated that the Eps15 homology (EH) domain of EHD1 binds to phosphoinositides, including phosphatidylinositol-4-phosphate. Herein, we identify phosphatidylinositol-4-phosphate as an essential component of EHD1-associated tubules in vivo. Indeed, an EHD1 EH domain mutant (K483E) that associates exclusively with punctate membranes displayed decreased binding to phosphatidylinositol-4-phosphate and other phosphoinositides. Moreover, we provide evidence that although the tubular membranes to which EHD1 associates may be stabilized and/or enhanced by EHD1 expression, these membranes are, at least in part, pre-existing structures. Finally, to underscore the function of EHD1-containing tubules in vivo, we used a small interfering RNA (siRNA)/rescue assay. On transfection, wild-type, tubule-associated, siRNA-resistant EHD1 rescued transferrin and β1 integrin recycling defects observed in EHD1-depleted cells, whereas expression of the EHD1 K483E mutant did not. We propose that phosphatidylinositol-4-phosphate is an essential component of EHD1-associated tubules that also contain phosphatidylinositol-(4,5)-bisphosphate and that these structures are required for efficient recycling to the plasma membrane.

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Metadata

Authors
Jović, M., Kieken, F., Naslavsky, N., Sorgen, P. L., & Caplan, S.
Affiliations
Department of Biochemistry and Molecular Biology, and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, NE 68198-5870
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2009-06
Volume
20
Issue
11
Pages
2731-2743
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e08-11-1102
Cited by
81
References
2
Language
en

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