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© The Rockefeller University Press, 0021-9525/2000//901 $5.00
The Journal of Cell Biology, Volume 149, Number 4, , 2000 901-914

Original Article

Distinct Membrane Domains on Endosomes in the Recycling Pathway Visualized by Multicolor Imaging of Rab4, Rab5, and Rab11



Birte Sönnichsena, Stefano De Renzisa, Erik Nielsena, Jens Rietdorfb, and Marino Zeriala

a Max Planck Institute for Molecular Cell Biology and Genetics, 01307 Dresden, Germany
b Advanced Light Microscopy Facility, European Molecular Biology Laboratory, 69117 Heidelberg, Germany

sonnichs{at}embl-heidelberg.de

Two endosome populations involved in recycling of membranes and receptors to the plasma membrane have been described, the early and the recycling endosome. However, this distinction is mainly based on the flow of cargo molecules and the spatial distribution of these membranes within the cell. To get insights into the membrane organization of the recycling pathway, we have studied Rab4, Rab5, and Rab11, three regulatory components of the transport machinery. Following transferrin as cargo molecule and GFP-tagged Rab proteins we could show that cargo moves through distinct domains on endosomes. These domains are occupied by different Rab proteins, revealing compartmentalization within the same continuous membrane. Endosomes are comprised of multiple combinations of Rab4, Rab5, and Rab11 domains that are dynamic but do not significantly intermix over time. Three major populations were observed: one that contains only Rab5, a second with Rab4 and Rab5, and a third containing Rab4 and Rab11. These membrane domains display differential pharmacological sensitivity, reflecting their biochemical and functional diversity. We propose that endosomes are organized as a mosaic of different Rab domains created through the recruitment of specific effector proteins, which cooperatively act to generate a restricted environment on the membrane.

Key Words: endocytosis • transferrin recycling • Rab proteins • EEA1

© 2000 The Rockefeller University Press

The online version of this paper contains supplemental material.

Drs. Sönnichsen, De Renzis, Nielsen, and Zerial's current address is c/o European Molecular Biology Laboratory, 69117 Heidelberg, Germany.

Abbreviations used in this paper: EEA1, early endosomal antigen 1; PI(3)P, phosphoinositol-3-phosphate; VSV-G, vesicular stomatitis virus glycoprotein.


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