Transferrin receptor recycling in the absence of perinuclear recycling endosomes

In mammalian cells, internalized receptors such as transferrin (Tfn) receptor are presumed to pass sequentially through early endosomes (EEs) and perinuclear recycling endosomes (REs) before returning to the plasma membrane. Whether passage through RE is obligatory, however, remains unclear. Kinetic...

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Main Authors:	Sheff, David, Pelletier, Laurence, O'Connell, Christopher B., Warren, Graham, Mellman, Ira
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2002
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173326/

id	pubmed-2173326
recordtype	oai_dc
spelling	pubmed-21733262008-05-01 Transferrin receptor recycling in the absence of perinuclear recycling endosomes Sheff, David Pelletier, Laurence O'Connell, Christopher B. Warren, Graham Mellman, Ira Report In mammalian cells, internalized receptors such as transferrin (Tfn) receptor are presumed to pass sequentially through early endosomes (EEs) and perinuclear recycling endosomes (REs) before returning to the plasma membrane. Whether passage through RE is obligatory, however, remains unclear. Kinetic analysis of endocytosis in CHO cells suggested that the majority of internalized Tfn bypassed REs returning to the surface from EEs. To determine directly if REs are dispensable for recycling, we studied Tfn recycling in cytoplasts microsurgically created to contain peripheral EEs but to exclude perinuclear REs. The cytoplasts actively internalized and recycled Tfn. Surprisingly, they also exhibited spatially and temporally distinct endosome populations. The first appeared to correspond to EEs, labeling initially with Tfn, being positive for early endosomal antigen 1 (EEA-1) and containing only small amounts of Rab11, an RE marker. The second was EEA-1 negative and with time recruited Rab11, suggesting that cytoplasts assembled functional REs. These results suggest that although perinuclear REs are not essential components of the Tfn recycling pathway, they are dynamic structures which preexist in the peripheral cytoplasm or can be regenerated from EE- and cytosol-derived components such as Rab11. The Rockefeller University Press 2002-03-04 /pmc/articles/PMC2173326/ /pubmed/11877458 http://dx.doi.org/10.1083/jcb.20111048 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Sheff, David Pelletier, Laurence O'Connell, Christopher B. Warren, Graham Mellman, Ira
spellingShingle	Sheff, David Pelletier, Laurence O'Connell, Christopher B. Warren, Graham Mellman, Ira Transferrin receptor recycling in the absence of perinuclear recycling endosomes
author_facet	Sheff, David Pelletier, Laurence O'Connell, Christopher B. Warren, Graham Mellman, Ira
author_sort	Sheff, David
title	Transferrin receptor recycling in the absence of perinuclear recycling endosomes
title_short	Transferrin receptor recycling in the absence of perinuclear recycling endosomes
title_full	Transferrin receptor recycling in the absence of perinuclear recycling endosomes
title_fullStr	Transferrin receptor recycling in the absence of perinuclear recycling endosomes
title_full_unstemmed	Transferrin receptor recycling in the absence of perinuclear recycling endosomes
title_sort	transferrin receptor recycling in the absence of perinuclear recycling endosomes
description	In mammalian cells, internalized receptors such as transferrin (Tfn) receptor are presumed to pass sequentially through early endosomes (EEs) and perinuclear recycling endosomes (REs) before returning to the plasma membrane. Whether passage through RE is obligatory, however, remains unclear. Kinetic analysis of endocytosis in CHO cells suggested that the majority of internalized Tfn bypassed REs returning to the surface from EEs. To determine directly if REs are dispensable for recycling, we studied Tfn recycling in cytoplasts microsurgically created to contain peripheral EEs but to exclude perinuclear REs. The cytoplasts actively internalized and recycled Tfn. Surprisingly, they also exhibited spatially and temporally distinct endosome populations. The first appeared to correspond to EEs, labeling initially with Tfn, being positive for early endosomal antigen 1 (EEA-1) and containing only small amounts of Rab11, an RE marker. The second was EEA-1 negative and with time recruited Rab11, suggesting that cytoplasts assembled functional REs. These results suggest that although perinuclear REs are not essential components of the Tfn recycling pathway, they are dynamic structures which preexist in the peripheral cytoplasm or can be regenerated from EE- and cytosol-derived components such as Rab11.
publisher	The Rockefeller University Press
publishDate	2002
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173326/
_version_	1611425239288250368

Transferrin receptor recycling in the absence of perinuclear recycling endosomes

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