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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...
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Published in: | The Journal of biological chemistry 2006-07, Vol.281 (28), p.19417-19425 |
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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 |
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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. 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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). 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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 |
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