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Most newly synthesized peroxisomal matrix proteins are transported to the organelle by Pex5p, a remarkable multidomain protein involved in an intricate network of transient protein-protein interactions. Presently, our knowledge regarding the structure/function of amino acid residues 118 to the very last residue of mammalian Pex5p is quite vast. Indeed, the cargo-protein receptor domain as well as the binding sites for several peroxins have all been mapped to this region of Pex5p. In contrast, structural/functional data regarding the first 117 amino acid residues of Pex5p are still scarce. Here we show that a truncated Pex5p lacking the first 110 amino acid residues (ΔN110-Pex5p) displays exactly the peroxisomal import properties of the full-length peroxin implying that this N-terminal domain is involved neither in cargo-protein binding nor in the docking/translocation step of the Pex5p-cargo protein complex at the peroxisomal membrane. However, the ATP-dependent export step of ΔN110-Pex5p from the peroxisomal membrane is completely blocked, a phenomenon that was also observed for a Pex5p version lacking just the first 17 amino acid residues but not for a truncated protein comprising amino acid residues 1–324 of Pex5p. By exploring the unique properties of ΔN110-Pex5p, the effect of temperature on the import/export kinetics of Pex5p was characterized. Our data indicate that the export step of Pex5p from the peroxisomal compartment (in contrast with its insertion into the organelle membrane) is highly dependent on the temperature. Most newly synthesized peroxisomal matrix proteins are transported to the organelle by Pex5p, a remarkable multidomain protein involved in an intricate network of transient protein-protein interactions. Presently, our knowledge regarding the structure/function of amino acid residues 118 to the very last residue of mammalian Pex5p is quite vast. Indeed, the cargo-protein receptor domain as well as the binding sites for several peroxins have all been mapped to this region of Pex5p. In contrast, structural/functional data regarding the first 117 amino acid residues of Pex5p are still scarce. Here we show that a truncated Pex5p lacking the first 110 amino acid residues (ΔN110-Pex5p) displays exactly the peroxisomal import properties of the full-length peroxin implying that this N-terminal domain is involved neither in cargo-protein binding nor in the docking/translocation step of the Pex5p-cargo protein complex at the peroxisomal membrane. However, the ATP-dependent export step of ΔN110-Pex5p from the peroxisomal membrane is completely blocked, a phenomenon that was also observed for a Pex5p version lacking just the first 17 amino acid residues but not for a truncated protein comprising amino acid residues 1–324 of Pex5p. By exploring the unique properties of ΔN110-Pex5p, the effect of temperature on the import/export kinetics of Pex5p was characterized. Our data indicate that the export step of Pex5p from the peroxisomal compartment (in contrast with its insertion into the organelle membrane) is highly dependent on the temperature. All peroxisomal matrix proteins are synthesized in the cytosol and post-translationally imported into the organelle. Specific targeting of these proteins to the peroxisome is promoted by one of two receptor proteins, the peroxins Pex5p and Pex7p (reviewed in Refs. 1Purdue P.E. Lazarow P.B. Annu. Rev. Cell Dev. Biol. 2001; 17: 701-752Crossref PubMed Scopus (285) Google Scholar, 2Sparkes I.A. Baker A. Mol. Membr. Biol. 2002; 19: 171-185Crossref PubMed Scopus (34) Google Scholar, 3Eckert J.H. Erdmann R. Rev. Physiol. Biochem. Pharmacol. 2003; 147: 75-121Crossref PubMed Scopus (81) Google Scholar, 4Weller S. Gould S.J. Valle D. Annu. Rev. Genomics Hum. Genet. 2003; 4: 165-211Crossref PubMed Scopus (158) Google Scholar). By far the vast majority of peroxisomal matrix proteins use Pex5p as their import receptor. Proteins belonging to this family possess a peroxisomal targeting signal type 1 (PTS1), 1The abbreviations used are: PTS, peroxisomal targeting sequence; PNS, post-nuclear supernatant; MOPS, 4-morpholinepropanesulfonic acid; GST, glutathione S-transferase; TPRs, Pex5p domain (amino acid residues 312–639) comprising its tetratricopeptide repeats; ATPγS, adenosine 5′-O-(thiotriphosphate).1The abbreviations used are: PTS, peroxisomal targeting sequence; PNS, post-nuclear supernatant; MOPS, 4-morpholinepropanesulfonic acid; GST, glutathione S-transferase; TPRs, Pex5p domain (amino acid residues 312–639) comprising its tetratricopeptide repeats; ATPγS, adenosine 5′-O-(thiotriphosphate). a C-terminal tripeptide with the sequence SKL, or a conserved variant (5Gould S.J. Keller G.A. Hosken N. Wilkinson J. Subramani S. J. Cell Biol. 1989; 108: 1657-1664Crossref PubMed Scopus (880) Google Scholar, 6Miura S. Kasuya-Arai I. Mori H. Miyazawa S. Osumi T. Hashimoto T. Fujiki Y. J. Biol. Chem. 1992; 267: 14405-14411Abstract Full Text PDF PubMed Google Scholar, 7Lametschwandtner G. Brocard C. Fransen M. van Veldhoven P. Berger J. Hartig A. J. Biol. Chem. 1998; 273: 33635-33643Abstract Full Text Full Text PDF PubMed Scopus (165) Google Scholar). A very small group of peroxisomal matrix proteins is targeted to the organelle by Pex7p. This peroxin recognizes a degenerated nona-peptide complying to the consensus sequence (R/K)(L/I/V)X5(H/Q)(L/A/F), the so-called peroxisomal targeting signal type 2 (PTS2) (8Swinkels B.W. Gould S.J. Bodnar A.G. Rachubinski R.A. Subramani S. EMBO J. 1991; 10: 3255-3262Crossref PubMed Scopus (515) Google Scholar, 9Osumi T. Tsukamoto T. Hata S. Yokota S. Miura S. Fujiki Y. Hijikata M. Miyazawa S. Hashimoto T. Biochem. Biophys. Res. Commun. 1991; 181: 947-954Crossref PubMed Scopus (230) Google Scholar, 10Rehling P. M. M. EMBO J. PubMed Scopus Google Scholar). In and but not in targeting of these proteins to Pex5p, that the two import at the of the receptor N. G. Gould S.J. Valle D. Hum. Mol. Genet. 1998; PubMed Scopus Google Scholar, H. T. M. S. A. A. N. Fujiki Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, T. H. Fujiki Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, G. D. P. Gould S.J. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, M. M. Cell Physiol. 2002; PubMed Scopus Google Scholar, Lazarow P.B. J. Cell Biol. PubMed Scopus Google Scholar, Y. M. T. Subramani S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, P.E. Lazarow P.B. J. Cell Biol. 1998; PubMed Scopus Google Scholar, Rachubinski R.A. J. Cell Biol. 1998; PubMed Scopus Google Scholar, M. A. H. Erdmann R. H. Mol. Biol. 2003; PubMed Google Scholar, H. S. EMBO 2001; PubMed Scopus Google Scholar). protein import into (reviewed in Refs. 1Purdue P.E. Lazarow P.B. Annu. Rev. Cell Dev. Biol. 2001; 17: 701-752Crossref PubMed Scopus (285) Google Scholar, 2Sparkes I.A. Baker A. Mol. Membr. Biol. 2002; 19: 171-185Crossref PubMed Scopus (34) Google Scholar, 3Eckert J.H. Erdmann R. Rev. Physiol. Biochem. Pharmacol. 2003; 147: 75-121Crossref PubMed Scopus (81) Google Scholar, 4Weller S. Gould S.J. Valle D. Annu. Rev. Genomics Hum. Genet. 2003; 4: 165-211Crossref PubMed Scopus (158) Google Scholar). In the first newly synthesized peroxisomal proteins with their receptor still in the for this is well Indeed, and have that the tetratricopeptide in the C-terminal of Pex5p the binding for the sequence G. Brocard C. Fransen M. van Veldhoven P. Berger J. Hartig A. J. Biol. Chem. 1998; 273: 33635-33643Abstract Full Text Full Text PDF PubMed Scopus (165) Google Scholar, C. T. Hartig A. Biochem. Biophys. Res. Commun. PubMed Scopus Google Scholar, G. N. C. A. P. Valle D. Gould S.J. Genet. PubMed Scopus Google Scholar, M. C. M. van Veldhoven J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, D. Subramani S. EMBO J. PubMed Scopus Google Scholar, Gould S.J. Biol. PubMed Scopus Google Scholar, P. G. D. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar). In the these are by a complex protein at the peroxisomal membrane. the and of this are still protein that and are the of this protein complex M. M. J. Cell Biol. 2001; PubMed Scopus Google Scholar, C. C. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, H. P. A. Mol. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). or this proteins are the membrane of the peroxisome is still regarding the of Pex5p this Indeed, have that Pex5p is completely the organelle membrane with the proteins M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, M. van J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). However, data that Pex5p in with the peroxisomal membrane this step are also and J. C. Cell Biochem. Biophys. PubMed Scopus Google Scholar). Pex5p is to the cytosol in to of the that is at this R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google not is regarding this the data this are G. Gould S.J. J. Cell Biol. PubMed Scopus Google Scholar, Gould S.J. Mol. Biol. PubMed Scopus Google Scholar, Subramani S. 2001; Full Text Full Text PDF PubMed Scopus Google is that we are still far from the of this of we regarding this been from of peroxisomal Pex5p in several G. Gould S.J. J. Cell Biol. PubMed Scopus Google Scholar, Gould S.J. Mol. Biol. PubMed Scopus Google Scholar). is that this type of been quite in to involved in protein the peroxisomal membrane. However, is also that have to used in to in the of this have an in to the of of Pex5p with and from the peroxisomal of Pex5p with a post-nuclear from and the that Pex5p a into the peroxisomal membrane C. C. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). By this was that insertion of Pex5p into the peroxisomal membrane the of proteins in the import and on an membrane of the peroxisomal docking/translocation C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). insertion of Pex5p into the organelle membrane not that the for protein the peroxisomal membrane on protein-protein interactions. In contrast, export of Pex5p from the peroxisomal compartment is ATP-dependent R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the peroxisomal membrane two of Pex5p and C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). In the of in Pex5p and the peroxisomal peroxisomal Pex5p as a protein the majority of its into the peroxisomal with a small N-terminal of to the from the of the membrane. This is the so-called 2 Pex5p. or in the of a membrane of Pex5p is This of Pex5p, to as Pex5p, is completely to the as as the are was also that 2 is the of Pex5p and that this of Pex5p the peroxisomal membrane in the of Most 2 and Pex5p by to the that in with Pex5p of the not at the peroxisomal a that is in with the protein M. M. J. Cell Biol. 2001; PubMed Scopus Google Scholar, C. C. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, H. P. A. Mol. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). Here we have used this in to the of the first 110 amino acid residues of Pex5p. By several is that a truncated version of Pex5p lacking this domain displays exactly the peroxisomal import properties of the full-length version of the implying that this domain is neither for cargo-protein binding nor for insertion into the peroxisomal membrane. However, in contrast to full-length Pex5p, N-terminal truncated Pex5p is to the peroxisomal By the unique properties of this truncated version of Pex5p we have the import/export kinetics of full-length Pex5p. post-nuclear and as R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google in 1 with 2 In import or in import and 2 in a of an and was in the import this the Pex5p export of is for data not of import and of protein for and exactly as C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). full-length Pex5p N. G. Gould S.J. Valle D. Hum. Mol. Genet. 1998; PubMed Scopus Google or the C-terminal truncated version comprising amino acid residues 1–324 of Pex5p by the as C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar, C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the N-terminal truncated of Pex5p lacking the first 17 or the first 110 amino acid residues and ΔN110-Pex5p, by an 1991; 10: Google Scholar). In the first the C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google was by the or and the In the this was used with the to in proteins synthesized the in the of the In of or of with of or C. C. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google or of or M. T. C. van Veldhoven Mol. Biol. 2001; PubMed Scopus Google in of import for on the import by the and of glutathione a protein comprising to amino acid residues of Pex5p C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google a signal at the C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google and with a sequence; C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google proteins used in import at of and and and from protein to the of was the of was the Pex5p the 110 to the of mammalian Pex5p to as N. G. Gould S.J. Valle D. Hum. Mol. Genet. 1998; PubMed Scopus Google is a remarkable multidomain protein of amino acid residues involved in a complex network of transient protein-protein interactions. Presently, our knowledge on the structure/function of amino acid residues of mammalian Pex5p is quite vast. Indeed, a of and have that this region of the protein the binding for proteins G. Brocard C. Fransen M. van Veldhoven P. Berger J. Hartig A. J. Biol. Chem. 1998; 273: 33635-33643Abstract Full Text Full Text PDF PubMed Scopus (165) Google Scholar, C. T. Hartig A. Biochem. Biophys. Res. Commun. PubMed Scopus Google Scholar, G. N. C. A. P. Valle D. Gould S.J. Genet. PubMed Scopus Google Scholar, M. C. M. van Veldhoven J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, D. Subramani S. EMBO J. PubMed Scopus Google Scholar, Gould S.J. Biol. PubMed Scopus Google Scholar, P. G. D. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google J. G. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, J. G. A. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, H. M. T. N. Fujiki Y. Mol. Biol. 2002; PubMed Scopus Google and binding sites for Pex7p N. G. Gould S.J. Valle D. Hum. Mol. Genet. 1998; PubMed Scopus Google Scholar, H. T. M. S. A. A. N. Fujiki Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, T. H. Fujiki Y. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, G. D. P. Gould S.J. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Gould S.J. J. Cell Biol. 147: PubMed Scopus Google and H. M. T. N. Fujiki Y. Mol. Biol. 2002; PubMed Scopus Google Scholar). In contrast, not is regarding the of the first 117 amino acid residues of Pex5p. this domain is for the of Pex5p in was H. M. T. N. Fujiki Y. Mol. Biol. 2002; PubMed Scopus Google Scholar). However, the this In to this we have used an in import to the properties of a truncated version of Pex5p lacking the first 110 amino acid residues (ΔN110-Pex5p) with the by the full-length full-length Pex5p is to an import in the of two peroxisomal membrane of the peroxin are of the import to 2 Pex5p and Pex5p In the of 2 Pex5p is by far the In the of ATPγS, the two membrane of Pex5p are However, the of these are with in the of that this phenomenon not the for the import step of Pex5p. was that this step is R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). This is to the that import in the of the and This of export of Pex5p from the docking/translocation sites these sites for the Pex5p. the with ΔN110-Pex5p are two are first is that in the of or in the of is to two that the 2 and Pex5p is that the by a that amino acid residues C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). in the of this as is the for ΔN110-Pex5p, this is in with the membrane for 2 Pex5p C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). the of ΔN110-Pex5p in the and of this is with the one for the full-length is that ΔN110-Pex5p full-length Pex5p in an import this is insertion of full-length Pex5p into the peroxisomal membrane the of proteins in the import these proteins are from the by an of a protein comprising the receptor domain of Pex5p but not its peroxisomal targeting domain insertion of Pex5p into the organelle membrane is observed C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). used this to the import properties of in insertion of ΔN110-Pex5p into the peroxisomal membrane is is to the import and However, this effect is in the of an of a protein insertion of ΔN110-Pex5p into the peroxisomal membrane is used to the of this in on the use of an to of with this the of Pex5p that is into peroxisomal membrane C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). This that the import of a protein is also in the of M. Subramani S. S. A. 1998; PubMed Scopus Google Scholar). we the effect of on the membrane insertion of in the of ΔN110-Pex5p the is with the 1 and 2 with the observed not or to are used in these in insertion of Pex5p or ΔN110-Pex5p into the peroxisomal membrane is highly 1 and 2 with Most this effect of is still observed these two proteins are to import and with are not in the export of Pex5p to the compartment R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). this that not docking/translocation sites of the peroxisomal membrane these data indicate that insertion of ΔN110-Pex5p into the peroxisomal membrane is as as the insertion of the full-length In these data to that the first 110 amino acid residues of Pex5p not in cargo-protein binding or in the docking/translocation step of the Pex5p-cargo protein complex at the peroxisomal membrane. ΔN110-Pex5p a for the the of ΔN110-Pex5p in import in the of is the one observed for the full-length that these full-length Pex5p and the peroxisomal membrane R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google this to that the export step of ΔN110-Pex5p from the peroxisomal membrane this an in import was C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). full-length Pex5p and ΔN110-Pex5p, a C-terminal truncated protein comprising amino acid residues 1–324 of Pex5p was also in this import not the properties of C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). Pex5p, ΔN110-Pex5p, or with a for in the of this a vast of was to the import to import of the an of import was and was to the and the of peroxisomal Pex5p that Pex5p is of the peroxisomal membrane C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). 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Cell Biol. 2002; PubMed Scopus Google Scholar). is the of the of the Pex5p-cargo protein complex with the docking/translocation is in the of Our knowledge of the export step of Pex5p from the peroxisomal membrane is not been that is at this step R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google but the of the involved or the for is one to all these is to data regarding the kinetics of these Here the of temperature on the peroxisomal import/export of Pex5p are to this first is to the that in our in the of Pex5p is at not at C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google a the that Pex5p at the peroxisomal compartment in just by the temperature of the G. Gould S.J. J. Cell Biol. PubMed Scopus Google Scholar). 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In contrast, of Pex5p are at and that of 2 into Pex5p is In this we data regarding the peroxisomal protein import with on its last the ATP-dependent step of Pex5p. is that the first 110 amino acid residues of Pex5p are involved neither in cargo-protein binding nor in the docking/translocation step that at the peroxisomal membrane. the used to this one is for the first and This the effect of on the peroxisomal import step of Pex5p. is an membrane of the peroxisomal membrane involved in the step of Pex5p to the compartment H. M. T. N. Fujiki Y. Mol. Biol. 2002; PubMed Scopus Google Scholar, D. Gould S.J. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). In binding and and have that this peroxin is of with and Pex5p M. C. D. van Veldhoven Mol. 2002; 1 Full Text Full Text PDF PubMed Scopus Google Scholar). are that in the of with Pex5p is the regarding the Indeed, peroxisomal from and are with the of in with C. C. J. Biol. Chem. 2001; Full Text Full Text PDF PubMed Scopus Google Scholar, H. P. A. Mol. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). to these the is to the or is in a protein complex and still on the of protein the peroxisomal membrane H. P. A. Mol. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). that completely the insertion of Pex5p into the peroxisomal membrane that not docking/translocation sites of the peroxisomal membrane possess the first all the Pex5p protein data the that the first 110 amino acid residues of Pex5p are involved neither in cargo-protein binding nor in the docking/translocation step is not Indeed, ΔN110-Pex5p still the as well as all the binding sites for and (reviewed in Refs. 3Eckert J.H. Erdmann R. Rev. Physiol. Biochem. Pharmacol. 2003; 147: 75-121Crossref PubMed Scopus (81) Google and 4Weller S. Gould S.J. Valle D. Annu. Rev. Genomics Hum. Genet. 2003; 4: 165-211Crossref PubMed Scopus (158) Google Scholar). is the that ΔN110-Pex5p is not a for the peroxisomal export the export of Pex5p to the from this first the insertion step of Pex5p into the peroxisomal membrane. that the of ΔN110-Pex5p in our that this step is an the of Pex5p the export A two to the of Pex5p from the docking/translocation Pex5p a in this the the export of Pex5p from the peroxisomal membrane the docking/translocation its Pex5p an in this Pex5p from the docking/translocation by the By that a Pex5p domain with in the docking/translocation step is for the export of Pex5p from the peroxisomal our data this last at the Pex5p residues for the export step indicate that residues are not to export of Pex5p from the peroxisomal membrane. This that the first 17 amino acid residues of Pex5p a in this In this to the N-terminal of Pex5p is conserved the sequence is amino acid is at the of Pex5p proteins not is the that are at the of and Rachubinski R.A. J. Cell Biol. 1998; PubMed Scopus Google Scholar, M. A. H. Erdmann R. H. Mol. Biol. 2003; PubMed Google Scholar). This peroxin is to the receptor to the peroxisomal a that in and is by Pex5p Rachubinski R.A. J. Cell Biol. 1998; PubMed Scopus Google Scholar, M. A. H. Erdmann R. H. Mol. Biol. 2003; PubMed Google Scholar, H. S. EMBO 2001; PubMed Scopus Google Scholar). this N-terminal domain of is also for the export of this peroxin from the docking/translocation to these residues of Pex5p are for its However, that are to the of a an and the export of Pex5p on one and the first amino acid residues of Pex5p on the as is the that is not a for the export the that in our in Pex5p in the of or in the of C. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google the 2 and Pex5p in a effect by the the export step of Pex5p its first amino acid is that Pex5p in an in in full-length Pex5p is not from the peroxisomal membrane. was that the export in this in is or R.A. C. J. Biol. Chem. 2003; Full Text Full Text PDF PubMed Scopus Google Scholar). all these to the that the of Pex5p the binding for the its of the of Pex5p in the export step is also by the with this truncated protein amino acid residues 1–324 of Pex5p, our data show that is also a for the export This that the of Pex5p, a region that the cargo-protein binding is not involved in with the export the signal for the export not in at the C-terminal of Pex5p, the receptor its on the of the peroxisomal membrane. signal from the of Pex5p. is that at the of the step of the membrane peroxins in with the of Pex5p on the one the of Pex5p to its on the the Pex5p to these are in and in are of the docking/translocation that are involved in of the H. M. T. N. Fujiki Y. Mol. Biol. 2002; PubMed Scopus Google Scholar, D. Gould S.J. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar, P. A. T. M. Erdmann R. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). However, a is also is that at the of the step Pex5p the properties by the kinetics of the export step of Pex5p from the peroxisomal compartment was also characterized. is that this step is highly dependent on temperature. A of export was at at In contrast, insertion of Pex5p into the peroxisomal membrane at this temperature. data the for the that Pex5p at the peroxisomal compartment in just by the temperature of the G. Gould S.J. J. Cell Biol. PubMed Scopus Google Scholar). of Pex5p at the peroxisomal compartment not from a of the as but from a in the export step of Pex5p. In our in and in the in this at the step 2 Pex5p is into Pex5p. the that the export step of Pex5p from the peroxisomal compartment is quite at with the peroxisomal of Pex5p a we that the and the to By exploring the unique properties of ΔN110-Pex5p, is to the peroxisomal import and export of Pex5p. of on of these
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