Loading…

Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery

Pex19p is required for the topogenesis of peroxisomal membrane proteins (PMPs). Here we have demonstrated that Pex19p is also required for the peroxisomal targeting and stability of Pex17p, a peripheral component of the docking complex of the peroxisomal protein import machinery. We have demonstrate...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2006-07, Vol.281 (28), p.19417-19425
Main Authors: Girzalsky, Wolfgang, Hoffmann, Linda S., Schemenewitz, Andreas, Nolte, Andreas, Kunau, Wolf-Hubert, Erdmann, Ralf
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3
cites cdi_FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3
container_end_page 19425
container_issue 28
container_start_page 19417
container_title The Journal of biological chemistry
container_volume 281
creator Girzalsky, Wolfgang
Hoffmann, Linda S.
Schemenewitz, Andreas
Nolte, Andreas
Kunau, Wolf-Hubert
Erdmann, Ralf
description Pex19p is required for the topogenesis of peroxisomal membrane proteins (PMPs). Here we have demonstrated that Pex19p is also required for the peroxisomal targeting and stability of Pex17p, a peripheral component of the docking complex of the peroxisomal protein import machinery. We have demonstrated that Pex17p is associated with the peroxisomal Pex13p-Pex14p complex as well as with Pex19p. We have identified the corresponding binding sites for Pex14p and Pex19p and demonstrated that a specific loss of the Pex19p interaction resulted in mistargeting of Pex17p. We have shown that a construct consisting only of the Pex19p- and Pex14p-binding sites of Pex17p is sufficient to direct an otherwise cytosolic reporter protein to the peroxisomal membrane in a Pex19p-dependent manner. Our data show that the function of Pex19p as chaperone or import receptor is not restricted to integral membrane proteins but may also include peripheral PMPs. As a consequence of our data, the previous definition of a targeting signal for PMPs (mPTS) as a Pex19p-binding motif in conjunction with a transmembrane segment should be extended to regions comprising a Pex19p-binding motif and a peroxisomal anchor sequence.
doi_str_mv 10.1074/jbc.M603344200
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68624798</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819465034</els_id><sourcerecordid>17258405</sourcerecordid><originalsourceid>FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3</originalsourceid><addsrcrecordid>eNqFkc1r3DAQxUVpaTZprzkGH0pO8VYjyZZ1LEu-IKE5pNCbkOTxWmFtuZI3H_99texCTqWCQYL3m0HzHiGnQJdApfj-ZN3yvqacC8Eo_UAWQBte8gp-fyQLShmUilXNETlO6YnmIxR8JkdQ11JxgAXpH_AV1FS2OOHY4jgXjyaucfbjughdsVPldFGY_Ip-6jGaTbEKwxTGHZuJucedFl59CkMWH2KY0Y_FbWbiXNwb1_sR49sX8qkzm4RfD_cJ-XV1-bi6Ke9-Xt-uftyVLm8wl51RKG3HauYEq9A0WBtrAKXjSnJeW4eupYY60VoF2AluOceqsoZz5ljLT8j5fu4Uw58tplkPPjncbMyIYZt03dRMSNX8FwSZjRO0yuByD7oYUorY6Sn6wcQ3DVTvQtA5BP0eQm44O0ze2gHbd_zgega-7YHer_sXH1FbH1yPg2YN5NKgBMiMNXsMs1_PHqNOzuPosM0tbtZt8P_6wl_RGaIR</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17258405</pqid></control><display><type>article</type><title>Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery</title><source>ScienceDirect®</source><source>PubMed Central</source><creator>Girzalsky, Wolfgang ; Hoffmann, Linda S. ; Schemenewitz, Andreas ; Nolte, Andreas ; Kunau, Wolf-Hubert ; Erdmann, Ralf</creator><creatorcontrib>Girzalsky, Wolfgang ; Hoffmann, Linda S. ; Schemenewitz, Andreas ; Nolte, Andreas ; Kunau, Wolf-Hubert ; Erdmann, Ralf</creatorcontrib><description>Pex19p is required for the topogenesis of peroxisomal membrane proteins (PMPs). Here we have demonstrated that Pex19p is also required for the peroxisomal targeting and stability of Pex17p, a peripheral component of the docking complex of the peroxisomal protein import machinery. We have demonstrated that Pex17p is associated with the peroxisomal Pex13p-Pex14p complex as well as with Pex19p. We have identified the corresponding binding sites for Pex14p and Pex19p and demonstrated that a specific loss of the Pex19p interaction resulted in mistargeting of Pex17p. We have shown that a construct consisting only of the Pex19p- and Pex14p-binding sites of Pex17p is sufficient to direct an otherwise cytosolic reporter protein to the peroxisomal membrane in a Pex19p-dependent manner. Our data show that the function of Pex19p as chaperone or import receptor is not restricted to integral membrane proteins but may also include peripheral PMPs. As a consequence of our data, the previous definition of a targeting signal for PMPs (mPTS) as a Pex19p-binding motif in conjunction with a transmembrane segment should be extended to regions comprising a Pex19p-binding motif and a peroxisomal anchor sequence.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M603344200</identifier><identifier>PMID: 16679311</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Base Sequence ; Binding Sites ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Cytosol - metabolism ; Membrane Proteins - metabolism ; Membrane Transport Proteins ; Molecular Sequence Data ; Peroxins ; Peroxisomes - chemistry ; Protein Transport ; Repressor Proteins - metabolism ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; Signal Transduction ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2006-07, Vol.281 (28), p.19417-19425</ispartof><rights>2006 © 2006 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3</citedby><cites>FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0021925819465034$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3547,27923,27924,45779</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16679311$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Girzalsky, Wolfgang</creatorcontrib><creatorcontrib>Hoffmann, Linda S.</creatorcontrib><creatorcontrib>Schemenewitz, Andreas</creatorcontrib><creatorcontrib>Nolte, Andreas</creatorcontrib><creatorcontrib>Kunau, Wolf-Hubert</creatorcontrib><creatorcontrib>Erdmann, Ralf</creatorcontrib><title>Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Pex19p is required for the topogenesis of peroxisomal membrane proteins (PMPs). Here we have demonstrated that Pex19p is also required for the peroxisomal targeting and stability of Pex17p, a peripheral component of the docking complex of the peroxisomal protein import machinery. We have demonstrated that Pex17p is associated with the peroxisomal Pex13p-Pex14p complex as well as with Pex19p. We have identified the corresponding binding sites for Pex14p and Pex19p and demonstrated that a specific loss of the Pex19p interaction resulted in mistargeting of Pex17p. We have shown that a construct consisting only of the Pex19p- and Pex14p-binding sites of Pex17p is sufficient to direct an otherwise cytosolic reporter protein to the peroxisomal membrane in a Pex19p-dependent manner. Our data show that the function of Pex19p as chaperone or import receptor is not restricted to integral membrane proteins but may also include peripheral PMPs. As a consequence of our data, the previous definition of a targeting signal for PMPs (mPTS) as a Pex19p-binding motif in conjunction with a transmembrane segment should be extended to regions comprising a Pex19p-binding motif and a peroxisomal anchor sequence.</description><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cytosol - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins</subject><subject>Molecular Sequence Data</subject><subject>Peroxins</subject><subject>Peroxisomes - chemistry</subject><subject>Protein Transport</subject><subject>Repressor Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Signal Transduction</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkc1r3DAQxUVpaTZprzkGH0pO8VYjyZZ1LEu-IKE5pNCbkOTxWmFtuZI3H_99texCTqWCQYL3m0HzHiGnQJdApfj-ZN3yvqacC8Eo_UAWQBte8gp-fyQLShmUilXNETlO6YnmIxR8JkdQ11JxgAXpH_AV1FS2OOHY4jgXjyaucfbjughdsVPldFGY_Ip-6jGaTbEKwxTGHZuJucedFl59CkMWH2KY0Y_FbWbiXNwb1_sR49sX8qkzm4RfD_cJ-XV1-bi6Ke9-Xt-uftyVLm8wl51RKG3HauYEq9A0WBtrAKXjSnJeW4eupYY60VoF2AluOceqsoZz5ljLT8j5fu4Uw58tplkPPjncbMyIYZt03dRMSNX8FwSZjRO0yuByD7oYUorY6Sn6wcQ3DVTvQtA5BP0eQm44O0ze2gHbd_zgega-7YHer_sXH1FbH1yPg2YN5NKgBMiMNXsMs1_PHqNOzuPosM0tbtZt8P_6wl_RGaIR</recordid><startdate>20060714</startdate><enddate>20060714</enddate><creator>Girzalsky, Wolfgang</creator><creator>Hoffmann, Linda S.</creator><creator>Schemenewitz, Andreas</creator><creator>Nolte, Andreas</creator><creator>Kunau, Wolf-Hubert</creator><creator>Erdmann, Ralf</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060714</creationdate><title>Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery</title><author>Girzalsky, Wolfgang ; Hoffmann, Linda S. ; Schemenewitz, Andreas ; Nolte, Andreas ; Kunau, Wolf-Hubert ; Erdmann, Ralf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cytosol - metabolism</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Transport Proteins</topic><topic>Molecular Sequence Data</topic><topic>Peroxins</topic><topic>Peroxisomes - chemistry</topic><topic>Protein Transport</topic><topic>Repressor Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Signal Transduction</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Girzalsky, Wolfgang</creatorcontrib><creatorcontrib>Hoffmann, Linda S.</creatorcontrib><creatorcontrib>Schemenewitz, Andreas</creatorcontrib><creatorcontrib>Nolte, Andreas</creatorcontrib><creatorcontrib>Kunau, Wolf-Hubert</creatorcontrib><creatorcontrib>Erdmann, Ralf</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Girzalsky, Wolfgang</au><au>Hoffmann, Linda S.</au><au>Schemenewitz, Andreas</au><au>Nolte, Andreas</au><au>Kunau, Wolf-Hubert</au><au>Erdmann, Ralf</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2006-07-14</date><risdate>2006</risdate><volume>281</volume><issue>28</issue><spage>19417</spage><epage>19425</epage><pages>19417-19425</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Pex19p is required for the topogenesis of peroxisomal membrane proteins (PMPs). Here we have demonstrated that Pex19p is also required for the peroxisomal targeting and stability of Pex17p, a peripheral component of the docking complex of the peroxisomal protein import machinery. We have demonstrated that Pex17p is associated with the peroxisomal Pex13p-Pex14p complex as well as with Pex19p. We have identified the corresponding binding sites for Pex14p and Pex19p and demonstrated that a specific loss of the Pex19p interaction resulted in mistargeting of Pex17p. We have shown that a construct consisting only of the Pex19p- and Pex14p-binding sites of Pex17p is sufficient to direct an otherwise cytosolic reporter protein to the peroxisomal membrane in a Pex19p-dependent manner. Our data show that the function of Pex19p as chaperone or import receptor is not restricted to integral membrane proteins but may also include peripheral PMPs. As a consequence of our data, the previous definition of a targeting signal for PMPs (mPTS) as a Pex19p-binding motif in conjunction with a transmembrane segment should be extended to regions comprising a Pex19p-binding motif and a peroxisomal anchor sequence.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16679311</pmid><doi>10.1074/jbc.M603344200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 2006-07, Vol.281 (28), p.19417-19425
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_68624798
source ScienceDirect®; PubMed Central
subjects Base Sequence
Binding Sites
Carrier Proteins - metabolism
Cell Membrane - metabolism
Cytosol - metabolism
Membrane Proteins - metabolism
Membrane Transport Proteins
Molecular Sequence Data
Peroxins
Peroxisomes - chemistry
Protein Transport
Repressor Proteins - metabolism
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Signal Transduction
Two-Hybrid System Techniques
title Pex19p-dependent Targeting of Pex17p, a Peripheral Component of the Peroxisomal Protein Import Machinery
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-13T01%3A28%3A12IST&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=Pex19p-dependent%20Targeting%20of%20Pex17p,%20a%20Peripheral%20Component%20of%20the%20Peroxisomal%20Protein%20Import%20Machinery&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Girzalsky,%20Wolfgang&rft.date=2006-07-14&rft.volume=281&rft.issue=28&rft.spage=19417&rft.epage=19425&rft.pages=19417-19425&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M603344200&rft_dat=%3Cproquest_cross%3E17258405%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c442t-fa9e7bf262c425ea8e6aba1e7c397336bcecd0a0c4db91ef43b33e55ba332c2d3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=17258405&rft_id=info:pmid/16679311&rfr_iscdi=true