LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation

We recently showed that leucine-rich glioma inactivated 3 (LGI3) mediates the internalization of β-amyloid protein and transferrin, a well-known marker for clathrin-dependent endocytosis, in neural cells. These findings strongly suggest that LGI3 is involved in the endocytosis system in the brain; h...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Neuroreport 2010-06, Vol.21 (9), p.606-610
Hauptverfasser: Okabayashi, Sachi, Kimura, Nobuyuki
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 610
container_issue 9
container_start_page 606
container_title Neuroreport
container_volume 21
creator Okabayashi, Sachi
Kimura, Nobuyuki
description We recently showed that leucine-rich glioma inactivated 3 (LGI3) mediates the internalization of β-amyloid protein and transferrin, a well-known marker for clathrin-dependent endocytosis, in neural cells. These findings strongly suggest that LGI3 is involved in the endocytosis system in the brain; however, the precise function of LGI3 remains unclear. Here, we show that LGI3 interacts with flotillin-1 (Flo1), and RNA interference analysis shows that LGI3 stabilized Flo1, and Flo1 also stabilized LGI3 vice versa. Moreover, the downregulation of the LGI3/Flo1 complex altered β-amyloid precursor protein trafficking directly to late endosomes and disrupted exosome formation, suggesting that LGI3 is involved not only in endocytosis but also in another intracellular transport system through binding with its co-factor such as Flo1.
doi_str_mv 10.1097/WNR.0b013e3283383467
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_754903165</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>733137211</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3877-e6be383815326a7d38da95fbb16a81a732dd6214b89b7fb6085cdb86a7d278143</originalsourceid><addsrcrecordid>eNqFkE1P3DAURa0KVKbT_oOq8o5VwC8v_sgSIRhGGtERomp3kZ04jMGJwfZoyr9v0ACLLtrV25x779Mh5CuwE2C1PP15fXPCDAO0WCpEhZWQH8gMKokF5-rXAZmxmtdFVQt-RD6ldM8Yqxmoj-SoZJUAVuKMrFeLJVI3Zht1mxPdubyhvQ_Zee_GAmgOdLCd09nSs_Wa5qj73rUPbryjeuyo_R1SGCztQxx0dmH8TA577ZP98nrn5Mflxe35VbH6vlien62KFpWUhRXGTj8r4FgKLTtUna55bwwIrUBLLLtOlFAZVRvZG8EUbzujXtBSKqhwTo73vY8xPG1tys3gUmu916MN29RIXtUMQfD_k4iAsgSYyGpPtjGkFG3fPEY36PjcAGtepDeT9OZv6VPs2-vA1kyu3kNvlidA7YFd8JPo9OC3OxubjdU-b_7d_QeQf444</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733137211</pqid></control><display><type>article</type><title>LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation</title><source>MEDLINE</source><source>Journals@Ovid Complete</source><creator>Okabayashi, Sachi ; Kimura, Nobuyuki</creator><creatorcontrib>Okabayashi, Sachi ; Kimura, Nobuyuki</creatorcontrib><description>We recently showed that leucine-rich glioma inactivated 3 (LGI3) mediates the internalization of β-amyloid protein and transferrin, a well-known marker for clathrin-dependent endocytosis, in neural cells. These findings strongly suggest that LGI3 is involved in the endocytosis system in the brain; however, the precise function of LGI3 remains unclear. Here, we show that LGI3 interacts with flotillin-1 (Flo1), and RNA interference analysis shows that LGI3 stabilized Flo1, and Flo1 also stabilized LGI3 vice versa. Moreover, the downregulation of the LGI3/Flo1 complex altered β-amyloid precursor protein trafficking directly to late endosomes and disrupted exosome formation, suggesting that LGI3 is involved not only in endocytosis but also in another intracellular transport system through binding with its co-factor such as Flo1.</description><identifier>ISSN: 0959-4965</identifier><identifier>EISSN: 1473-558X</identifier><identifier>DOI: 10.1097/WNR.0b013e3283383467</identifier><identifier>PMID: 20461023</identifier><language>eng</language><publisher>England: Lippincott Williams &amp; Wilkins, Inc</publisher><subject>Amyloid beta-Protein Precursor - metabolism ; Animals ; Biological Transport ; Brain - metabolism ; Cell Line, Tumor ; Cell Membrane - metabolism ; Endocytosis - physiology ; Exosomes - metabolism ; Immunoprecipitation ; Membrane Proteins - metabolism ; Mice ; Mice, Inbred C57BL ; Nerve Tissue Proteins - metabolism ; Neurons - metabolism ; Protein Stability ; RNA Interference</subject><ispartof>Neuroreport, 2010-06, Vol.21 (9), p.606-610</ispartof><rights>2010 Lippincott Williams &amp; Wilkins, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3877-e6be383815326a7d38da95fbb16a81a732dd6214b89b7fb6085cdb86a7d278143</citedby><cites>FETCH-LOGICAL-c3877-e6be383815326a7d38da95fbb16a81a732dd6214b89b7fb6085cdb86a7d278143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20461023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okabayashi, Sachi</creatorcontrib><creatorcontrib>Kimura, Nobuyuki</creatorcontrib><title>LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation</title><title>Neuroreport</title><addtitle>Neuroreport</addtitle><description>We recently showed that leucine-rich glioma inactivated 3 (LGI3) mediates the internalization of β-amyloid protein and transferrin, a well-known marker for clathrin-dependent endocytosis, in neural cells. These findings strongly suggest that LGI3 is involved in the endocytosis system in the brain; however, the precise function of LGI3 remains unclear. Here, we show that LGI3 interacts with flotillin-1 (Flo1), and RNA interference analysis shows that LGI3 stabilized Flo1, and Flo1 also stabilized LGI3 vice versa. Moreover, the downregulation of the LGI3/Flo1 complex altered β-amyloid precursor protein trafficking directly to late endosomes and disrupted exosome formation, suggesting that LGI3 is involved not only in endocytosis but also in another intracellular transport system through binding with its co-factor such as Flo1.</description><subject>Amyloid beta-Protein Precursor - metabolism</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Brain - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane - metabolism</subject><subject>Endocytosis - physiology</subject><subject>Exosomes - metabolism</subject><subject>Immunoprecipitation</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons - metabolism</subject><subject>Protein Stability</subject><subject>RNA Interference</subject><issn>0959-4965</issn><issn>1473-558X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1P3DAURa0KVKbT_oOq8o5VwC8v_sgSIRhGGtERomp3kZ04jMGJwfZoyr9v0ACLLtrV25x779Mh5CuwE2C1PP15fXPCDAO0WCpEhZWQH8gMKokF5-rXAZmxmtdFVQt-RD6ldM8Yqxmoj-SoZJUAVuKMrFeLJVI3Zht1mxPdubyhvQ_Zee_GAmgOdLCd09nSs_Wa5qj73rUPbryjeuyo_R1SGCztQxx0dmH8TA577ZP98nrn5Mflxe35VbH6vlien62KFpWUhRXGTj8r4FgKLTtUna55bwwIrUBLLLtOlFAZVRvZG8EUbzujXtBSKqhwTo73vY8xPG1tys3gUmu916MN29RIXtUMQfD_k4iAsgSYyGpPtjGkFG3fPEY36PjcAGtepDeT9OZv6VPs2-vA1kyu3kNvlidA7YFd8JPo9OC3OxubjdU-b_7d_QeQf444</recordid><startdate>20100623</startdate><enddate>20100623</enddate><creator>Okabayashi, Sachi</creator><creator>Kimura, Nobuyuki</creator><general>Lippincott Williams &amp; Wilkins, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7TK</scope></search><sort><creationdate>20100623</creationdate><title>LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation</title><author>Okabayashi, Sachi ; Kimura, Nobuyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3877-e6be383815326a7d38da95fbb16a81a732dd6214b89b7fb6085cdb86a7d278143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amyloid beta-Protein Precursor - metabolism</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>Brain - metabolism</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane - metabolism</topic><topic>Endocytosis - physiology</topic><topic>Exosomes - metabolism</topic><topic>Immunoprecipitation</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons - metabolism</topic><topic>Protein Stability</topic><topic>RNA Interference</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okabayashi, Sachi</creatorcontrib><creatorcontrib>Kimura, Nobuyuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Neurosciences Abstracts</collection><jtitle>Neuroreport</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okabayashi, Sachi</au><au>Kimura, Nobuyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation</atitle><jtitle>Neuroreport</jtitle><addtitle>Neuroreport</addtitle><date>2010-06-23</date><risdate>2010</risdate><volume>21</volume><issue>9</issue><spage>606</spage><epage>610</epage><pages>606-610</pages><issn>0959-4965</issn><eissn>1473-558X</eissn><abstract>We recently showed that leucine-rich glioma inactivated 3 (LGI3) mediates the internalization of β-amyloid protein and transferrin, a well-known marker for clathrin-dependent endocytosis, in neural cells. These findings strongly suggest that LGI3 is involved in the endocytosis system in the brain; however, the precise function of LGI3 remains unclear. Here, we show that LGI3 interacts with flotillin-1 (Flo1), and RNA interference analysis shows that LGI3 stabilized Flo1, and Flo1 also stabilized LGI3 vice versa. Moreover, the downregulation of the LGI3/Flo1 complex altered β-amyloid precursor protein trafficking directly to late endosomes and disrupted exosome formation, suggesting that LGI3 is involved not only in endocytosis but also in another intracellular transport system through binding with its co-factor such as Flo1.</abstract><cop>England</cop><pub>Lippincott Williams &amp; Wilkins, Inc</pub><pmid>20461023</pmid><doi>10.1097/WNR.0b013e3283383467</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0959-4965
ispartof Neuroreport, 2010-06, Vol.21 (9), p.606-610
issn 0959-4965
1473-558X
language eng
recordid cdi_proquest_miscellaneous_754903165
source MEDLINE; Journals@Ovid Complete
subjects Amyloid beta-Protein Precursor - metabolism
Animals
Biological Transport
Brain - metabolism
Cell Line, Tumor
Cell Membrane - metabolism
Endocytosis - physiology
Exosomes - metabolism
Immunoprecipitation
Membrane Proteins - metabolism
Mice
Mice, Inbred C57BL
Nerve Tissue Proteins - metabolism
Neurons - metabolism
Protein Stability
RNA Interference
title LGI3 interacts with flotillin-1 to mediate APP trafficking and exosome formation
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-16T19%3A27%3A52IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=LGI3%20interacts%20with%20flotillin-1%20to%20mediate%20APP%20trafficking%20and%20exosome%20formation&rft.jtitle=Neuroreport&rft.au=Okabayashi,%20Sachi&rft.date=2010-06-23&rft.volume=21&rft.issue=9&rft.spage=606&rft.epage=610&rft.pages=606-610&rft.issn=0959-4965&rft.eissn=1473-558X&rft_id=info:doi/10.1097/WNR.0b013e3283383467&rft_dat=%3Cproquest_cross%3E733137211%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=733137211&rft_id=info:pmid/20461023&rfr_iscdi=true