The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment
Integrating the pleomorphic membranes of the intermediate compartment (IC) into the array of Golgi cisternae is a crucial step in membrane transport, but it is poorly understood. To gain insight into this step, we investigated the dynamics by which cis -Golgi matrix proteins such as GM130 and GRASP6...
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Veröffentlicht in: | Nature cell biology 2001-12, Vol.3 (12), p.1101-1113 |
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creator | Marra, Pierfrancesco Maffucci, Tania Daniele, Tiziana Tullio, Giuseppe Di Ikehara, Yukio Chan, Edward K. L Luini, Alberto Beznoussenko, Gala Mironov, Alexander De Matteis, Maria Antonietta |
description | Integrating the pleomorphic membranes of the intermediate compartment (IC) into the array of Golgi cisternae is a crucial step in membrane transport, but it is poorly understood. To gain insight into this step, we investigated the dynamics by which
cis
-Golgi matrix proteins such as GM130 and GRASP65 associate with, and incorporate, incoming IC elements. We found that GM130 and GRASP65 cycle via membranous tubules between the Golgi complex and a constellation of mobile structures that we call late IC stations. These stations are intermediate between the IC and the
cis
-Golgi in terms of composition, and they receive cargo from earlier IC elements and deliver it to the Golgi complex. Late IC elements are transient in nature and sensitive to fixatives; they are seen in only a fraction of fixed cells, whereas they are always visible in living cells. Finally, late IC stations undergo homotypic fusion and establish tubular connections between themselves and the Golgi. Overall, these features indicate that late IC stations mediate the transition between IC elements and the
cis
-Golgi face. |
doi_str_mv | 10.1038/ncb1201-1101 |
format | Article |
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cis
-Golgi matrix proteins such as GM130 and GRASP65 associate with, and incorporate, incoming IC elements. We found that GM130 and GRASP65 cycle via membranous tubules between the Golgi complex and a constellation of mobile structures that we call late IC stations. These stations are intermediate between the IC and the
cis
-Golgi in terms of composition, and they receive cargo from earlier IC elements and deliver it to the Golgi complex. Late IC elements are transient in nature and sensitive to fixatives; they are seen in only a fraction of fixed cells, whereas they are always visible in living cells. Finally, late IC stations undergo homotypic fusion and establish tubular connections between themselves and the Golgi. Overall, these features indicate that late IC stations mediate the transition between IC elements and the
cis
-Golgi face.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb1201-1101</identifier><identifier>PMID: 11781572</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Autoantigens ; Biology ; Biomedical and Life Sciences ; Cancer Research ; Cell Biology ; Cell Compartmentation - physiology ; Cellular proteins ; COS Cells ; Developmental Biology ; Genetic aspects ; Golgi apparatus ; Golgi Apparatus - chemistry ; Golgi Apparatus - metabolism ; Golgi Apparatus - ultrastructure ; Golgi Matrix Proteins ; Green Fluorescent Proteins ; Indicators and Reagents - metabolism ; Life Sciences ; Luminescent Proteins - genetics ; Membrane Glycoproteins ; Membrane Proteins - analysis ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Physiological aspects ; Protein Transport - physiology ; Proteins ; Secretory Vesicles - chemistry ; Secretory Vesicles - metabolism ; Stem Cells ; Transfection ; Viral Envelope Proteins - metabolism</subject><ispartof>Nature cell biology, 2001-12, Vol.3 (12), p.1101-1113</ispartof><rights>Springer Nature Limited 2001</rights><rights>COPYRIGHT 2001 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Dec 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c546t-de1ea1f503c07d7b595556e6b2b64b0b25a17b269788e59d807f2f9ac17916d83</citedby><cites>FETCH-LOGICAL-c546t-de1ea1f503c07d7b595556e6b2b64b0b25a17b269788e59d807f2f9ac17916d83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11781572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marra, Pierfrancesco</creatorcontrib><creatorcontrib>Maffucci, Tania</creatorcontrib><creatorcontrib>Daniele, Tiziana</creatorcontrib><creatorcontrib>Tullio, Giuseppe Di</creatorcontrib><creatorcontrib>Ikehara, Yukio</creatorcontrib><creatorcontrib>Chan, Edward K. L</creatorcontrib><creatorcontrib>Luini, Alberto</creatorcontrib><creatorcontrib>Beznoussenko, Gala</creatorcontrib><creatorcontrib>Mironov, Alexander</creatorcontrib><creatorcontrib>De Matteis, Maria Antonietta</creatorcontrib><title>The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Integrating the pleomorphic membranes of the intermediate compartment (IC) into the array of Golgi cisternae is a crucial step in membrane transport, but it is poorly understood. To gain insight into this step, we investigated the dynamics by which
cis
-Golgi matrix proteins such as GM130 and GRASP65 associate with, and incorporate, incoming IC elements. We found that GM130 and GRASP65 cycle via membranous tubules between the Golgi complex and a constellation of mobile structures that we call late IC stations. These stations are intermediate between the IC and the
cis
-Golgi in terms of composition, and they receive cargo from earlier IC elements and deliver it to the Golgi complex. Late IC elements are transient in nature and sensitive to fixatives; they are seen in only a fraction of fixed cells, whereas they are always visible in living cells. Finally, late IC stations undergo homotypic fusion and establish tubular connections between themselves and the Golgi. Overall, these features indicate that late IC stations mediate the transition between IC elements and the
cis
-Golgi face.</description><subject>Animals</subject><subject>Autoantigens</subject><subject>Biology</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell Compartmentation - physiology</subject><subject>Cellular proteins</subject><subject>COS Cells</subject><subject>Developmental Biology</subject><subject>Genetic aspects</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - chemistry</subject><subject>Golgi Apparatus - metabolism</subject><subject>Golgi Apparatus - ultrastructure</subject><subject>Golgi Matrix Proteins</subject><subject>Green Fluorescent Proteins</subject><subject>Indicators and Reagents - metabolism</subject><subject>Life Sciences</subject><subject>Luminescent Proteins - genetics</subject><subject>Membrane Glycoproteins</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Microscopy, Immunoelectron</subject><subject>Molecular Sequence Data</subject><subject>Physiological aspects</subject><subject>Protein Transport - physiology</subject><subject>Proteins</subject><subject>Secretory Vesicles - chemistry</subject><subject>Secretory Vesicles - metabolism</subject><subject>Stem Cells</subject><subject>Transfection</subject><subject>Viral Envelope Proteins - metabolism</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kl1rFDEUhgdR7IfeeS1BoSA4NSczSWYul6JroaK09TpkMmd2U2aSbZIB--_Nuot1RclFwslzXs7HWxSvgJ4DrZoPznTAKJQAFJ4Ux1BLUdZCtk-3b8FLWbXsqDiJ8Y5SqGsqnxdHALIBLtlxYW_XSJZfoKJEu54srxc33wQnSz-uLNkEn9C6SMyDGZGkdfDzav0L7HGwDokmce56P2nriB8ygcS6hGHC3uqExPhpo0Oa0KUXxbNBjxFf7u_T4vunj7cXn8urr8vLi8VVaXgtUtkjoIaB08pQ2cuOt5xzgaJjnag72jGuQXZMtLJpkLd9Q-XAhlYbkC2IvqlOi7Odbq7-fsaY1GSjwXHUDv0clWR5IFTwDL75C7zzc3C5NsUYq4SUlGbo7Q5a6RGVdYNPQZutolpAU7GmgmYrdf4PKp8eJ2u8y8PK8YOEdwcJmUn4I630HKO6vLk-ZN_vWBN8jAEHtQl20uFBAVVbC6i9BdTWAhl_vW9r7vIaHuH9zjNQ7oCYv9wKw2Pf_xHcz8npNAf8Lfin8aqf8MbBSw</recordid><startdate>20011201</startdate><enddate>20011201</enddate><creator>Marra, Pierfrancesco</creator><creator>Maffucci, Tania</creator><creator>Daniele, Tiziana</creator><creator>Tullio, Giuseppe Di</creator><creator>Ikehara, Yukio</creator><creator>Chan, Edward K. 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L</au><au>Luini, Alberto</au><au>Beznoussenko, Gala</au><au>Mironov, Alexander</au><au>De Matteis, Maria Antonietta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2001-12-01</date><risdate>2001</risdate><volume>3</volume><issue>12</issue><spage>1101</spage><epage>1113</epage><pages>1101-1113</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Integrating the pleomorphic membranes of the intermediate compartment (IC) into the array of Golgi cisternae is a crucial step in membrane transport, but it is poorly understood. To gain insight into this step, we investigated the dynamics by which
cis
-Golgi matrix proteins such as GM130 and GRASP65 associate with, and incorporate, incoming IC elements. We found that GM130 and GRASP65 cycle via membranous tubules between the Golgi complex and a constellation of mobile structures that we call late IC stations. These stations are intermediate between the IC and the
cis
-Golgi in terms of composition, and they receive cargo from earlier IC elements and deliver it to the Golgi complex. Late IC elements are transient in nature and sensitive to fixatives; they are seen in only a fraction of fixed cells, whereas they are always visible in living cells. Finally, late IC stations undergo homotypic fusion and establish tubular connections between themselves and the Golgi. Overall, these features indicate that late IC stations mediate the transition between IC elements and the
cis
-Golgi face.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11781572</pmid><doi>10.1038/ncb1201-1101</doi><tpages>13</tpages></addata></record> |
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subjects | Animals Autoantigens Biology Biomedical and Life Sciences Cancer Research Cell Biology Cell Compartmentation - physiology Cellular proteins COS Cells Developmental Biology Genetic aspects Golgi apparatus Golgi Apparatus - chemistry Golgi Apparatus - metabolism Golgi Apparatus - ultrastructure Golgi Matrix Proteins Green Fluorescent Proteins Indicators and Reagents - metabolism Life Sciences Luminescent Proteins - genetics Membrane Glycoproteins Membrane Proteins - analysis Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Microscopy, Immunoelectron Molecular Sequence Data Physiological aspects Protein Transport - physiology Proteins Secretory Vesicles - chemistry Secretory Vesicles - metabolism Stem Cells Transfection Viral Envelope Proteins - metabolism |
title | The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment |
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