Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum

The quality of cargo proteins in the endoplasmic reticulum (ER) is affected by their motion during folding. To understand how the diffusion of secretory cargo proteins is regulated in the ER, we directly analyze the motion of a single cargo molecule using fluorescence imaging/fluctuation analyses. W...

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Main Authors:	Nagaya, Hisao, Tamura, Taku, Higa-Nishiyama, Arisa, Ohashi, Koji, Takeuchi, Mayumi, Hashimoto, Hitoshi, Hatsuzawa, Kiyotaka, Kinjo, Masataka, Okada, Tatsuya, Wada, Ikuo
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2008
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213621/

id	pubmed-2213621
recordtype	oai_dc
spelling	pubmed-22136212008-07-14 Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum Nagaya, Hisao Tamura, Taku Higa-Nishiyama, Arisa Ohashi, Koji Takeuchi, Mayumi Hashimoto, Hitoshi Hatsuzawa, Kiyotaka Kinjo, Masataka Okada, Tatsuya Wada, Ikuo Research Articles The quality of cargo proteins in the endoplasmic reticulum (ER) is affected by their motion during folding. To understand how the diffusion of secretory cargo proteins is regulated in the ER, we directly analyze the motion of a single cargo molecule using fluorescence imaging/fluctuation analyses. We find that the addition of two N-glycans onto the cargo dramatically alters their diffusion by transient binding to membrane components that are confined by hyperosmolarity. Via simultaneous observation of a single cargo and ER exit sites (ERESs), we could exclude ERESs as the binding sites. Remarkably, actin cytoskeleton was required for the transient binding. These results provide a molecular basis for hypertonicity-induced immobilization of cargo, which is dependent on glycosylation at multiple sites but not the completion of proper folding. We propose that diffusion of secretory glycoproteins in the ER lumen is controlled from the cytoplasm to reduce the chances of aggregation. The Rockefeller University Press 2008-01-14 /pmc/articles/PMC2213621/ /pubmed/18195104 http://dx.doi.org/10.1083/jcb.200704078 Text en Copyright © 2008, 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	Nagaya, Hisao Tamura, Taku Higa-Nishiyama, Arisa Ohashi, Koji Takeuchi, Mayumi Hashimoto, Hitoshi Hatsuzawa, Kiyotaka Kinjo, Masataka Okada, Tatsuya Wada, Ikuo
spellingShingle	Nagaya, Hisao Tamura, Taku Higa-Nishiyama, Arisa Ohashi, Koji Takeuchi, Mayumi Hashimoto, Hitoshi Hatsuzawa, Kiyotaka Kinjo, Masataka Okada, Tatsuya Wada, Ikuo Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
author_facet	Nagaya, Hisao Tamura, Taku Higa-Nishiyama, Arisa Ohashi, Koji Takeuchi, Mayumi Hashimoto, Hitoshi Hatsuzawa, Kiyotaka Kinjo, Masataka Okada, Tatsuya Wada, Ikuo
author_sort	Nagaya, Hisao
title	Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
title_short	Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
title_full	Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
title_fullStr	Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
title_full_unstemmed	Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
title_sort	regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum
description	The quality of cargo proteins in the endoplasmic reticulum (ER) is affected by their motion during folding. To understand how the diffusion of secretory cargo proteins is regulated in the ER, we directly analyze the motion of a single cargo molecule using fluorescence imaging/fluctuation analyses. We find that the addition of two N-glycans onto the cargo dramatically alters their diffusion by transient binding to membrane components that are confined by hyperosmolarity. Via simultaneous observation of a single cargo and ER exit sites (ERESs), we could exclude ERESs as the binding sites. Remarkably, actin cytoskeleton was required for the transient binding. These results provide a molecular basis for hypertonicity-induced immobilization of cargo, which is dependent on glycosylation at multiple sites but not the completion of proper folding. We propose that diffusion of secretory glycoproteins in the ER lumen is controlled from the cytoplasm to reduce the chances of aggregation.
publisher	The Rockefeller University Press
publishDate	2008
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2213621/
_version_	1611434790590873600

Regulated motion of glycoproteins revealed by direct visualization of a single cargo in the endoplasmic reticulum

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