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Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells
Abstract
RME-1 is an Eps15-homology (EH)-domain protein that was identified in a genetic screen for endocytosis genes in Caenorhabditis elegans. When expressed in a CHO cell line, the worm RME-1 protein and a mouse homologue are both associated with the endocytic recycling compartment. Here we show that expression of a dominant-negative construct with a point mutation near the EH domain results in redistribution of the endocytic recycling compartment and slowing down of transferrin receptor recycling. The delivery of a TGN38 chimaeric protein to the trans-Golgi network is also slowed down. The function of Rme-1 in endocytic recycling is evolutionarily conserved in metazoans as shown by the protein's properties in C. elegans.
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EHD1 plays a critical role in recycling of plasma membrane receptors (e.g., transferrin) internalized through clathrin-coated pits or independently of clathrin.
“EHD1 [14] has been found to play a critical role in the recycling of plasma membrane receptors (ie., transferrin) that are internalized either through clathrin-coated pits [15-17], or independently of clathrin (MHC-I or β1 integrins) [18,19].”
From EHD1 regulates cholesterol homeostasis and lipid droplet storage (2007) · cites this paper as [19]
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Metadata
- Authors
- Lin, S. X., Grant, B., Hirsh, D., & Maxfield, F. R.
- Venue
- Nature Cell Biology
- Published
- 2001-05-14
- Volume
- 3
- Issue
- 6
- Pages
- 567-572
- ISSN
- 1465-7392
- 1476-4679
- Cited by
- 226
- References
- 0
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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