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Article: Endocytosis of adiponectin receptor 1 through a clathrin- and Rab5-dependent pathway

TitleEndocytosis of adiponectin receptor 1 through a clathrin- and Rab5-dependent pathway
Authors
KeywordsSpecies Index: Eukaryota
Issue Date2009
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.html
Citation
Cell Research, 2009, v. 19 n. 3, p. 317-327 How to Cite?
AbstractIn eukaryotic cells, receptor endocytosis is a key event regulating signaling transduction. Adiponectin receptors belong to a new receptor family that is distinct from G-protein-coupled receptors and has critical roles in the pathogenesis of diabetes and metabolic syndrome. Here, we analyzed the endocytosis of adiponectin and adiponectin receptor 1 (AdipoR1) and found that they are both internalized into transferrin-positive compartments that follow similar traffic routes. Blocking clathrin-mediated endocytosis by expressing Eps15 mutants or depleting K + trapped AdipoR1 at the plasma membrane, and K + depletion abolished adiponectin internalization, indicating that the endocytosis of AdipoR1 and adiponectin is clathrin-dependent. Depletion of K + and overexpression of Eps15 mutants enhance adiponectin-stimulated AMP-activated protein kinase phosphorylation, suggesting that the endocytosis of AdipoR1 might downregulate adiponectin signaling. In addition, AdipoR1 colocalizes with the small GTPase Rab5, and a dominant negative Rab5 abrogates AdipoR1 endocytosis. These data indicate that AdipoR1 is internalized through a clathrin- and Rab5-dependent pathway and that endocytosis may play a role in the regulation of adiponectin signaling. © 2009 IBCB, SIBS, CAS All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/92090
ISSN
2015 Impact Factor: 14.812
2015 SCImago Journal Rankings: 4.805
ISI Accession Number ID
Funding AgencyGrant Number
Chinese Academy of SciencesKSCX1-YW-02
National Natural Science Foundation of China30588002
Science & Technology Commission of Shanghai Municipality06XD14022
07DJ14005
Ministry of Science and Technology of China2006CB503900
2007CB947100
Funding Information:

We wish to thank Dr Alexandre Benmerah (Institut Cochin, Departement Maladies Infectieuses Paris F-75014, France) for providing the plasmids. This work was supported by research grants from the Chinese Academy of Sciences (One Hundred Talents Program and the Knowledge Innovation Program KSCX1-YW-02), the National Natural Science Foundation of China (30588002), Science & Technology Commission of Shanghai Municipality (06XD14022 and 07DJ14005), and the Ministry of Science and Technology of China (2006CB503900 and 2007CB947100) to Yan Chen.

References

 

DC FieldValueLanguage
dc.contributor.authorDing, Qen_HK
dc.contributor.authorWang, Zen_HK
dc.contributor.authorChen, Yen_HK
dc.date.accessioned2010-09-17T10:35:47Z-
dc.date.available2010-09-17T10:35:47Z-
dc.date.issued2009en_HK
dc.identifier.citationCell Research, 2009, v. 19 n. 3, p. 317-327en_HK
dc.identifier.issn1001-0602en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92090-
dc.description.abstractIn eukaryotic cells, receptor endocytosis is a key event regulating signaling transduction. Adiponectin receptors belong to a new receptor family that is distinct from G-protein-coupled receptors and has critical roles in the pathogenesis of diabetes and metabolic syndrome. Here, we analyzed the endocytosis of adiponectin and adiponectin receptor 1 (AdipoR1) and found that they are both internalized into transferrin-positive compartments that follow similar traffic routes. Blocking clathrin-mediated endocytosis by expressing Eps15 mutants or depleting K + trapped AdipoR1 at the plasma membrane, and K + depletion abolished adiponectin internalization, indicating that the endocytosis of AdipoR1 and adiponectin is clathrin-dependent. Depletion of K + and overexpression of Eps15 mutants enhance adiponectin-stimulated AMP-activated protein kinase phosphorylation, suggesting that the endocytosis of AdipoR1 might downregulate adiponectin signaling. In addition, AdipoR1 colocalizes with the small GTPase Rab5, and a dominant negative Rab5 abrogates AdipoR1 endocytosis. These data indicate that AdipoR1 is internalized through a clathrin- and Rab5-dependent pathway and that endocytosis may play a role in the regulation of adiponectin signaling. © 2009 IBCB, SIBS, CAS All rights reserved.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cr/marketing/index.htmlen_HK
dc.relation.ispartofCell Researchen_HK
dc.subjectSpecies Index: Eukaryotaen_HK
dc.titleEndocytosis of adiponectin receptor 1 through a clathrin- and Rab5-dependent pathwayen_HK
dc.typeArticleen_HK
dc.identifier.emailChen, Y:ychenc@hkucc.hku.hken_HK
dc.identifier.authorityChen, Y=rp1318en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/cr.2008.299en_HK
dc.identifier.pmid18982021-
dc.identifier.scopuseid_2-s2.0-61849184242en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-61849184242&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume19en_HK
dc.identifier.issue3en_HK
dc.identifier.spage317en_HK
dc.identifier.epage327en_HK
dc.identifier.eissn1748-7838-
dc.identifier.isiWOS:000265700000007-

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