Role of Galectins in Protein Trafficking
The galectins, a family of lectins, modulate distinct cellular processes, such as cancer progression, immune response and cellular development, through their specific binding to extracellular or intracellular ligands. In the past few years, research has unravelled interactions of different galectins...
Gespeichert in:
Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2009-10, Vol.10 (10), p.1405-1413 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 1413 |
---|---|
container_issue | 10 |
container_start_page | 1405 |
container_title | Traffic (Copenhagen, Denmark) |
container_volume | 10 |
creator | Delacour, Delphine Koch, Annett Jacob, Ralf |
description | The galectins, a family of lectins, modulate distinct cellular processes, such as cancer progression, immune response and cellular development, through their specific binding to extracellular or intracellular ligands. In the past few years, research has unravelled interactions of different galectins with lipids and glycoproteins in the outer milieu or in the secretory pathway of cells. Interestingly, these lectins do not possess a signalling sequence to enter the endoplasmic reticulum as a starting point for the classical secretory pathway. Instead they use a so-called non-classical mechanism for translocation across the plasma membrane and/or into the lumen of transport vesicles. Here, they stabilize transport platforms for apical trafficking or sort apical glycoproteins into specific vesicle populations. Modes of ligand interaction as well as the modulation of binding activities and trafficking pathways are discussed in this review. |
doi_str_mv | 10.1111/j.1600-0854.2009.00960.x |
format | Article |
fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_00493282v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>733669439</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5410-2ca1c351686aae3750da69fc110127fd655bf5e84cb1603a96c527999ef5af3b3</originalsourceid><addsrcrecordid>eNqNkNFOwjAUhhujEUVfQXenXmyetmu3Jt4QomBCokG4bkppsTgYrqDw9naO4K1NmnPSfv9p8yEUYUhwWPfzBHOAGHKWJgRAJGFzSLZH6OxwcRx6KvJYECxa6Nz7OQAQlqanqIUFZ4HBZ-h2WBYmKm3UU4XRa7f0kVtGr1W5NqGOKmWt0x9uObtAJ1YV3lzuaxuNnx5H3X48eOk9dzuDWLMUQ0y0wpoyzHOulKEZg6niwmqMAZPMTjljE8tMnupJ-ClVgmtGMiGEsUxZOqFtdNfMfVeFXFVuoaqdLJWT_c5A1mcAqaAkJ184sDcNu6rKz43xa7lwXpuiUEtTbrzMKOVcpFQEMm9IXZXeV8YeRmOQtVI5l7U5WZuTtVL5q1RuQ_Rq_8hmsjDTv-DeYQAeGuDbFWb378FyNOyEJsSvm7hVpVSzynk5fiOAKWCeZZwC_QGDZYp1</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>733669439</pqid></control><display><type>article</type><title>Role of Galectins in Protein Trafficking</title><source>Wiley Free Content</source><source>MEDLINE</source><source>IngentaConnect Free/Open Access Journals</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Delacour, Delphine ; Koch, Annett ; Jacob, Ralf</creator><creatorcontrib>Delacour, Delphine ; Koch, Annett ; Jacob, Ralf</creatorcontrib><description>The galectins, a family of lectins, modulate distinct cellular processes, such as cancer progression, immune response and cellular development, through their specific binding to extracellular or intracellular ligands. In the past few years, research has unravelled interactions of different galectins with lipids and glycoproteins in the outer milieu or in the secretory pathway of cells. Interestingly, these lectins do not possess a signalling sequence to enter the endoplasmic reticulum as a starting point for the classical secretory pathway. Instead they use a so-called non-classical mechanism for translocation across the plasma membrane and/or into the lumen of transport vesicles. Here, they stabilize transport platforms for apical trafficking or sort apical glycoproteins into specific vesicle populations. Modes of ligand interaction as well as the modulation of binding activities and trafficking pathways are discussed in this review.</description><identifier>ISSN: 1398-9219</identifier><identifier>EISSN: 1600-0854</identifier><identifier>DOI: 10.1111/j.1600-0854.2009.00960.x</identifier><identifier>PMID: 19650851</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Animals ; apical trafficking ; Cell Membrane ; Cell Membrane - metabolism ; Cellular Biology ; galectin ; Galectins ; Galectins - metabolism ; Galectins - physiology ; Galectins - secretion ; Glycoproteins ; Glycoproteins - metabolism ; Humans ; Life Sciences ; Ligands ; non-classical secretion ; Protein Binding ; protein clustering ; Protein Transport</subject><ispartof>Traffic (Copenhagen, Denmark), 2009-10, Vol.10 (10), p.1405-1413</ispartof><rights>2009 John Wiley & Sons A/S</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5410-2ca1c351686aae3750da69fc110127fd655bf5e84cb1603a96c527999ef5af3b3</citedby><cites>FETCH-LOGICAL-c5410-2ca1c351686aae3750da69fc110127fd655bf5e84cb1603a96c527999ef5af3b3</cites><orcidid>0000-0001-8202-4425</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1600-0854.2009.00960.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1600-0854.2009.00960.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19650851$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00493282$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Delacour, Delphine</creatorcontrib><creatorcontrib>Koch, Annett</creatorcontrib><creatorcontrib>Jacob, Ralf</creatorcontrib><title>Role of Galectins in Protein Trafficking</title><title>Traffic (Copenhagen, Denmark)</title><addtitle>Traffic</addtitle><description>The galectins, a family of lectins, modulate distinct cellular processes, such as cancer progression, immune response and cellular development, through their specific binding to extracellular or intracellular ligands. In the past few years, research has unravelled interactions of different galectins with lipids and glycoproteins in the outer milieu or in the secretory pathway of cells. Interestingly, these lectins do not possess a signalling sequence to enter the endoplasmic reticulum as a starting point for the classical secretory pathway. Instead they use a so-called non-classical mechanism for translocation across the plasma membrane and/or into the lumen of transport vesicles. Here, they stabilize transport platforms for apical trafficking or sort apical glycoproteins into specific vesicle populations. Modes of ligand interaction as well as the modulation of binding activities and trafficking pathways are discussed in this review.</description><subject>Animals</subject><subject>apical trafficking</subject><subject>Cell Membrane</subject><subject>Cell Membrane - metabolism</subject><subject>Cellular Biology</subject><subject>galectin</subject><subject>Galectins</subject><subject>Galectins - metabolism</subject><subject>Galectins - physiology</subject><subject>Galectins - secretion</subject><subject>Glycoproteins</subject><subject>Glycoproteins - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Ligands</subject><subject>non-classical secretion</subject><subject>Protein Binding</subject><subject>protein clustering</subject><subject>Protein Transport</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkNFOwjAUhhujEUVfQXenXmyetmu3Jt4QomBCokG4bkppsTgYrqDw9naO4K1NmnPSfv9p8yEUYUhwWPfzBHOAGHKWJgRAJGFzSLZH6OxwcRx6KvJYECxa6Nz7OQAQlqanqIUFZ4HBZ-h2WBYmKm3UU4XRa7f0kVtGr1W5NqGOKmWt0x9uObtAJ1YV3lzuaxuNnx5H3X48eOk9dzuDWLMUQ0y0wpoyzHOulKEZg6niwmqMAZPMTjljE8tMnupJ-ClVgmtGMiGEsUxZOqFtdNfMfVeFXFVuoaqdLJWT_c5A1mcAqaAkJ184sDcNu6rKz43xa7lwXpuiUEtTbrzMKOVcpFQEMm9IXZXeV8YeRmOQtVI5l7U5WZuTtVL5q1RuQ_Rq_8hmsjDTv-DeYQAeGuDbFWb378FyNOyEJsSvm7hVpVSzynk5fiOAKWCeZZwC_QGDZYp1</recordid><startdate>200910</startdate><enddate>200910</enddate><creator>Delacour, Delphine</creator><creator>Koch, Annett</creator><creator>Jacob, Ralf</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><general>Wiley</general><scope>FBQ</scope><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>1XC</scope><orcidid>https://orcid.org/0000-0001-8202-4425</orcidid></search><sort><creationdate>200910</creationdate><title>Role of Galectins in Protein Trafficking</title><author>Delacour, Delphine ; Koch, Annett ; Jacob, Ralf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5410-2ca1c351686aae3750da69fc110127fd655bf5e84cb1603a96c527999ef5af3b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>apical trafficking</topic><topic>Cell Membrane</topic><topic>Cell Membrane - metabolism</topic><topic>Cellular Biology</topic><topic>galectin</topic><topic>Galectins</topic><topic>Galectins - metabolism</topic><topic>Galectins - physiology</topic><topic>Galectins - secretion</topic><topic>Glycoproteins</topic><topic>Glycoproteins - metabolism</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Ligands</topic><topic>non-classical secretion</topic><topic>Protein Binding</topic><topic>protein clustering</topic><topic>Protein Transport</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Delacour, Delphine</creatorcontrib><creatorcontrib>Koch, Annett</creatorcontrib><creatorcontrib>Jacob, Ralf</creatorcontrib><collection>AGRIS</collection><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>Hyper Article en Ligne (HAL)</collection><jtitle>Traffic (Copenhagen, Denmark)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Delacour, Delphine</au><au>Koch, Annett</au><au>Jacob, Ralf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Galectins in Protein Trafficking</atitle><jtitle>Traffic (Copenhagen, Denmark)</jtitle><addtitle>Traffic</addtitle><date>2009-10</date><risdate>2009</risdate><volume>10</volume><issue>10</issue><spage>1405</spage><epage>1413</epage><pages>1405-1413</pages><issn>1398-9219</issn><eissn>1600-0854</eissn><abstract>The galectins, a family of lectins, modulate distinct cellular processes, such as cancer progression, immune response and cellular development, through their specific binding to extracellular or intracellular ligands. In the past few years, research has unravelled interactions of different galectins with lipids and glycoproteins in the outer milieu or in the secretory pathway of cells. Interestingly, these lectins do not possess a signalling sequence to enter the endoplasmic reticulum as a starting point for the classical secretory pathway. Instead they use a so-called non-classical mechanism for translocation across the plasma membrane and/or into the lumen of transport vesicles. Here, they stabilize transport platforms for apical trafficking or sort apical glycoproteins into specific vesicle populations. Modes of ligand interaction as well as the modulation of binding activities and trafficking pathways are discussed in this review.</abstract><cop>Oxford, UK</cop><pub>Oxford, UK : Blackwell Publishing Ltd</pub><pmid>19650851</pmid><doi>10.1111/j.1600-0854.2009.00960.x</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-8202-4425</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1398-9219 |
ispartof | Traffic (Copenhagen, Denmark), 2009-10, Vol.10 (10), p.1405-1413 |
issn | 1398-9219 1600-0854 |
language | eng |
recordid | cdi_hal_primary_oai_HAL_hal_00493282v1 |
source | Wiley Free Content; MEDLINE; IngentaConnect Free/Open Access Journals; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
subjects | Animals apical trafficking Cell Membrane Cell Membrane - metabolism Cellular Biology galectin Galectins Galectins - metabolism Galectins - physiology Galectins - secretion Glycoproteins Glycoproteins - metabolism Humans Life Sciences Ligands non-classical secretion Protein Binding protein clustering Protein Transport |
title | Role of Galectins in Protein Trafficking |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T14%3A29%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Role%20of%20Galectins%20in%20Protein%20Trafficking&rft.jtitle=Traffic%20(Copenhagen,%20Denmark)&rft.au=Delacour,%20Delphine&rft.date=2009-10&rft.volume=10&rft.issue=10&rft.spage=1405&rft.epage=1413&rft.pages=1405-1413&rft.issn=1398-9219&rft.eissn=1600-0854&rft_id=info:doi/10.1111/j.1600-0854.2009.00960.x&rft_dat=%3Cproquest_hal_p%3E733669439%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=733669439&rft_id=info:pmid/19650851&rfr_iscdi=true |