The Dynamin-like GTPase DLP1 Is Essential for Peroxisome Division and Is Recruited to Peroxisomes in Part by PEX11

Peroxisome division involves the conserved PEX11 peroxisomal membrane proteins and in yeast has been shown to require Vps1p, a dynamin-like protein. We show here that DLP1, the human homolog of the yeast DNM1and VPS1 genes, plays an important role in peroxisome division in human cells. Disruption of DLP1 function by either RNA interference or overexpressing dominant negativeDLP1 mutants causes a dramatic reduction in peroxisome abundance, although overexpression of functional DLP1 has no effect on peroxisome abundance. Overexpression of PEX11 induces peroxisome division in a multistep process involving elongation of preexisting peroxisomes followed by their division. We find that DLP1 is dispensable for the first phase of this process but essential for the second. Furthermore, we show that DLP1 associates with peroxisomes and that PEX11 overexpression recruits DLP1 to peroxisome membranes. However, we were unable to detect physical interaction between PEX11 and DLP1, and the stoichiometry of PEX11 and peroxisome-associated DLP1 was far less than 1:1. Based on these and other aspects, we propose that DLP1 performs an essential but transient role in peroxisome division and that PEX11 promotes peroxisome division by recruiting DLP1 to peroxisome membranes through an indirect mechanism. Peroxisome division involves the conserved PEX11 peroxisomal membrane proteins and in yeast has been shown to require Vps1p, a dynamin-like protein. We show here that DLP1, the human homolog of the yeast DNM1and VPS1 genes, plays an important role in peroxisome division in human cells. Disruption of DLP1 function by either RNA interference or overexpressing dominant negativeDLP1 mutants causes a dramatic reduction in peroxisome abundance, although overexpression of functional DLP1 has no effect on peroxisome abundance. Overexpression of PEX11 induces peroxisome division in a multistep process involving elongation of preexisting peroxisomes followed by their division. We find that DLP1 is dispensable for the first phase of this process but essential for the second. Furthermore, we show that DLP1 associates with peroxisomes and that PEX11 overexpression recruits DLP1 to peroxisome membranes. However, we were unable to detect physical interaction between PEX11 and DLP1, and the stoichiometry of PEX11 and peroxisome-associated DLP1 was far less than 1:1. Based on these and other aspects, we propose that DLP1 performs an essential but transient role in peroxisome division and that PEX11 promotes peroxisome division by recruiting DLP1 to peroxisome membranes through an indirect mechanism. peroxin dynamin-like protein 1 Dulbecco's modified phosphate-buffered saline green fluorescent protein hemagglutinin mouse embryonic fibroblasts peroxisomal membrane protein peroxisomes per section small interfering RNA The regulation of organelle abundance involves a complex interplay of organelle synthesis and destruction. In the case of peroxisomes, little is known about how cells control these competing processes. Peroxisome destruction appears to occur by a specialized form of autophagy (pexophagy) which requires most APG/CVTgenes. In addition to the APG/CVT genes that are involved in general autophagy, some specific factors are required for pexophagy (1Kim J. Klionsky D.J. Annu. Rev. Biochem. 2000; 69: 303-342Crossref PubMed Scopus (318) Google Scholar). Peroxisome formation appears to be even more complex. Many lines of evidence suggest that peroxisomes are formed mainly from preexisting peroxisomes, either by budding or fission, and this may be the predominant mechanism for peroxisome formation (2Lazarow P.B. Fujiki Y. Annu. Rev. Cell Biol. 1985; 1: 489-530Crossref PubMed Scopus (876) Google Scholar, 3Purdue P.E. Lazarow P.B. Annu. Rev. Cell Dev. Biol. 2001; 17: 701-752Crossref PubMed Scopus (285) Google Scholar). However, peroxisome synthesis has also been observed in the absence of preexisting peroxisomes (4South S.T. Sacksteder K.A. Li X. Liu Y. Gould S.J. J. Cell Biol. 2000; 149: 1345-1360Crossref PubMed Scopus (119) Google Scholar, 5South S.T. Baumgart E. Gould S.J. Proc. Natl. Acad. Sci. U. S. A. 2001; 98: 12027-12031Crossref PubMed Scopus (50) Google Scholar), indicating that there may be two parallel pathways for peroxisome formation, one from preexisting peroxisome and another de novo pathway for peroxisome formation (4South S.T. Sacksteder K.A. Li X. Liu Y. Gould S.J. J. Cell Biol. 2000; 149: 1345-1360Crossref PubMed Scopus (119) Google Scholar, 6Sacksteder K.A. Gould S.J. Annu. Rev. Genet. 2000; 34: 623-652Crossref PubMed Scopus (98) Google Scholar). Of the many PEX1genes and products (peroxins) required for peroxisome biogenesis, onlyPEX11 has been shown to have a conserved role in peroxisome division (7Erdmann R. Blobel G. J. Cell Biol. 1995; 128: 509-523Crossref PubMed Scopus (230) Google Scholar, 8Marshall P. Krimkevich Y. Lark R. Dyer J. Veenhuis M. Goodman J. J. Cell Biol. 1995; 129: 345-355Crossref PubMed Scopus (173) Google Scholar, 9Sakai Y. Marshall P.A. Saiganji A. Takabe K. Saiki H. Kato N. Goodman J.M. J. 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Cell Biol. 1995; 128: 509-523Crossref PubMed Scopus (230) Google Scholar, 8Marshall P. Krimkevich Y. Lark R. Dyer J. Veenhuis M. Goodman J. J. Cell Biol. 1995; 129: 345-355Crossref PubMed Scopus (173) Google Scholar, 12Schrader M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. Chem. 1998; 273: 29607-29614Abstract Full Text Full Text PDF PubMed Scopus (215) Google Scholar, 14Li X. Baumgart E. Morrell J.C. Jimenez-Sanchez G. Valle D. Gould S.J. Mol. Cell. Biol. 2002; 22: 4358-4365Crossref PubMed Scopus (133) Google Scholar). There is also evidence for metabolic control of peroxisome division (6Sacksteder K.A. Gould S.J. Annu. Rev. Genet. 2000; 34: 623-652Crossref PubMed Scopus (98) Google Scholar, 15Poll-The B.T. Roels F. Ogier H. Scotto J. Vamecq J. Schutgens R.B.H. Wanders R.J.A. Van Roermund C.W.T. Van Wyland M.J.A. Schram A.W. Tager J.M. Saudubray J.M. Am. J. Hum. Genet. 1988; 42: 422-434PubMed Google Scholar, 16Chang C.C. South S. Warren D. Jones J. Moser A.B. Moser H.W. Gould S.J. J. Cell Sci. 1999; 112: 1579-1590Crossref PubMed Google Scholar), although PEX11 proteins can induce peroxisome proliferation independently of peroxisome metabolism (17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). These results indicate that PEX11 proteins may play a positive role in the division process. In human cells, PEX11-mediated peroxisome division involves three steps: first, the import of PEX11 into the peroxisome membrane; second, the elongation of peroxisomes and the segregation of PEX11 proteins away from other peroxisomal membrane proteins, forming PEX11-enriched patches; and third, the division of elongated peroxisome tubules into multiple, small peroxisome vesicles (12Schrader M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. Chem. 1998; 273: 29607-29614Abstract Full Text Full Text PDF PubMed Scopus (215) Google Scholar, 17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). However, the biochemical activities of PEX11 proteins remain obscure, and there is as yet no mechanistic model for PEX11-induced peroxisome division. There may also be species-specific differences in PEX11 function because mammalian cells express at least three distinct PEX11 genes, whereasSaccharomyces cerevisiae has a single PEX11 gene (18Li X. Baumgart E. Dong G.X. Morrell J.C. Jimenez-Sanchez G. Valle D. Smith K.D. Gould S.G. Mol. Cell. Biol. 2002; 22: 8226-8240Crossref PubMed Scopus (125) Google Scholar). Recently, Hoepfner et al. (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google that the yeast Vps1p, is also involved in peroxisome division. mutants one or two peroxisomes and peroxisome abundance that induce PEX11 and peroxisome division (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google Scholar). a process in mammalian cells and to this is to PEX11-mediated peroxisome division, we the role of human DLP1 in peroxisome DLP1 is the human gene most to two of three dynamin-like proteins in and DLP1 is also known to the of and the Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, Y. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar). We here that a reduction in DLP1 peroxisome division and peroxisome abundance. Furthermore, we evidence that PEX11 overexpression recruits DLP1 to peroxisomes, a mechanism for PEX11-induced peroxisome division. The M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. 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The human DLP1 gene was by the RNA of human fibroblasts with a to the of human DLP1 for and two and for The products were with and of a in a modified from were and three of DLP1 and have been in The DLP1 gene was by the into the The dominant of and were by the and and and The were and and to their in and were by and Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar). the of DLP1 was by with and have been (4South S.T. Sacksteder K.A. Li X. Liu Y. Gould S.J. J. Cell Biol. 2000; 149: 1345-1360Crossref PubMed Scopus (119) Google Scholar). The to the were from the of the G. J.M. Mol. Cell. Biol. 1985; PubMed Scopus Google Scholar). to the and to were from the were from specific for and mouse were from human and the and mouse embryonic fibroblasts X. Baumgart E. Morrell J.C. Jimenez-Sanchez G. Valle D. Gould S.J. Mol. Cell. Biol. 2002; 22: 4358-4365Crossref PubMed Scopus (133) Google were M. G. S. Moser A.B. Moser H.W. Gould S.J. J. Cell Sci. 1995; PubMed Google Scholar). were by C.C. Moser H.W. Valle D. Gould S.J. Genet. PubMed Scopus Google Scholar). cells were in in Dulbecco's modified phosphate-buffered for and in in for were with for in with for in and on Peroxisome abundance in fibroblasts was as (17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). the of DLP1 in fibroblasts by RNA two of small interfering RNA and and one of were by and to the of was into fibroblasts from one by C.C. Moser H.W. Valle D. Gould S.J. Genet. PubMed Scopus Google Scholar), and the DLP1 protein and peroxisome and abundance were at by and indirect the peroxisome of in cells, fibroblasts were first or and for with with another of were for an the peroxisome abundance and the of DLP1 with peroxisomes, fibroblasts the or in with were by in 1 and and by through a were to at for to The was in 1 and was by of a of to into of the with The was with at for and were by with 1 of and in The and were by to and with the interaction between PEX11 proteins as as that between PEX11 and DLP1, fibroblasts the proteins were by with in or at for 1 were to at for to membranes. The was into with and was by either of a of or of a of protein of and with at for The were 1 with with 1 with 1 and with and 1 with The were in with by and with either or the of DLP1 with peroxisomes, fibroblasts or were by with and with 1 and 1 the cells were in of with and by through a were for at to a The was on of of with a of of and at for at were and for and as S.J. Biol. Scholar). in this were on S. cerevisiae The was as (17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). The was by of the in as the A. E. Li J. P. 1998; PubMed Scopus Google Scholar). The was from by of the VPS1 gene as the were the C. to and Scholar). were in yeast with or or as were with and as required C. to and Scholar). The that yeast in peroxisome membrane division that the human of have a However, the human DLP1 gene which is the human protein that the cerevisiae Vps1p, even cerevisiae a yeast protein that division and but has no role in peroxisome division (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google Scholar, H. J. Cell Biol. 1999; PubMed Scopus Google Scholar). Furthermore, human DLP1 has been shown to division and Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, Y. Mol. Biol. Cell. 1999; PubMed Scopus Google Scholar), indicating that more functional with than with was essential to human DLP1 has a role in peroxisome We first to DLP1 and DLP1 protein small interfering RNA specific for of DLP1 and and a control of a gene were to et al. J. A. K. T. 2001; PubMed Scopus Google Scholar). were into an human by were at and for and indirect at DLP1 is known to have that are by of the DLP1 Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, T. Y. H. Y. T. M. J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus (50) Google Scholar). that at least two were in fibroblasts The results also that were to DLP1 protein and the reduction of was by on the other no effect on the DLP1 protein that the is about for the in these cells, DLP1 protein are to be even than of in cells that the to peroxisome abundance in cells was to that of cells with the control However, cells with the peroxisomes Furthermore, the of peroxisomes in these cells was with peroxisomes in these cells a and with the of peroxisomes with to the peroxisomal that peroxisomal protein import was even in the cells with the most of peroxisome abundance an of DLP1 in peroxisome division, we and dominant DLP1 mutants in human fibroblasts and their on peroxisome abundance. DLP1 a of with in the have two dominant mutants that reduced and reduced B. Y. A. 2001; PubMed Scopus Google Scholar). We the in the DLP1 and of of DLP1 by Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, T. Y. H. Y. T. M. J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus (50) Google and of these single mutants of were into human was for indirect specific for the and an peroxisomal membrane protein Peroxisome abundance in cells was to that in cells first two and the form of to be and the other the peroxisome abundance was reduced in cells the which has a reduced for B. Y. A. 2001; PubMed Scopus Google Scholar). to the DLP1 RNA interference cells, some of the cells have a of peroxisomes and to be protein Overexpression of the also reduced peroxisome abundance in these cells However, this DLP1 to be with small of which to be peroxisomes and of and DLP1 have that these may as budding and organelle by membrane tubules PubMed Scopus Google Scholar, Cell. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar). to peroxisome division, this model that DLP1 associates with peroxisomes their division. for DLP1 of peroxisomes, we the of DLP1 and for the DLP1 proteins in small vesicles in fibroblasts the of vesicles were a small of vesicles also with the peroxisomal membrane protein by the of DLP1 with peroxisomes the division we of the that overexpression of PEX11 proteins induces peroxisome division. We protein in fibroblasts and specific for DLP1 and to detect DLP1 We also the to and the to these more DLP1 was with peroxisomes, and some DLP1 were the elongated peroxisome tubules to their division by that PEX11-mediated peroxisome division appears to peroxisome elongation and subsequent division (12Schrader M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. Chem. 1998; 273: 29607-29614Abstract Full Text Full Text PDF PubMed Scopus (215) Google Scholar, 17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar), these suggest that DLP1 associates with peroxisomes to or the division process. However, this interaction is to be transient because the of DLP1 with We we biochemical evidence for peroxisome-associated We cells with a to express a dominant to of with membrane B. Y. A. 2001; PubMed Scopus Google and a The were from cells, and the peroxisomal membranes were with We to detect and that was with peroxisome membranes a control for the of peroxisomal membranes to parallel were with cells with and was also into peroxisomes and no effect on peroxisome abundance in fibroblasts control that of DLP1 with peroxisomes was with a of was and the Furthermore, results were other peroxisomal membrane proteins were for of peroxisomal membranes of DLP1 with peroxisomes, we to peroxisomes from human fibroblasts that were with or peroxisome were by and with an that a DLP1 from the of this protein Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar), and specific for a peroxisomal membrane protein The of peroxisome-associated DLP1 was in cells with that DLP1 is to peroxisomes division. of peroxisome-associated DLP1 was also with of peroxisome membranes We with or in cells, the cells and peroxisome membranes with The were by the of peroxisome-associated DLP1 was about in cells than in control cells The of DLP1 to peroxisomes by the that DLP1 is required for peroxisome this we reduced DLP1 in human fibroblasts with the these cells with the to induce peroxisome division. Overexpression of a in peroxisome abundance in cells or cells with the control for In PEX11 overexpression was unable to induce peroxisome proliferation in cells with for In the cells with protein peroxisome elongation but induce peroxisome division overexpression to the segregation of peroxisome membrane into that were either in proteins or were in other peroxisomal membrane proteins and the is shown in the of results were also observed dominant DLP1 mutants were the between DLP1 and PEX11-mediated peroxisome division, we the or dominant into mouse embryonic The peroxisomes in the cells were with for the and or and In cells, the of no effect on either peroxisome abundance or and of on the other reduction of peroxisome abundance and peroxisome elongation X. Baumgart E. Morrell J.C. Jimenez-Sanchez G. Valle D. Gould S.J. Mol. Cell. Biol. 2002; 22: 4358-4365Crossref PubMed Scopus (133) Google Scholar), peroxisomes were reduced in abundance by about and of in this and was by Hoepfner et al. (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google that peroxisome abundance was reduced in of of the of and in peroxisome division, we the peroxisome in yeast mutants either or was to the we peroxisome abundance in these on which to peroxisome abundance, and which induces peroxisome abundance peroxisomes are the of and are required for on as R. Veenhuis M. D. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google the abundance of peroxisomes in the S. cerevisiae is (17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). was observed a of and the of peroxisome abundance. However, even with this is that the peroxisome abundance cells were from to and many in loss of PEX11 the in peroxisome abundance which in to However, a reduction in peroxisome abundance on of in reduced peroxisome abundance and also peroxisome proliferation as shown by the by Hoepfner et al. (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google Scholar). there were peroxisomes peroxisome abundance to be reduced even by the loss of PEX11 and VPS1 and We also overexpression of PEX11 be to peroxisome division in the absence of this we the with two an with or the with the by the which was to induce peroxisome proliferation in the in we that peroxisome abundance was in evidence that the PEX11-mediated peroxisome proliferation requires We have shown that DLP1 in PEX11-mediated peroxisome by peroxisome division. we to there is a physical between DLP1 and PEX11 We first for PEX11 proteins from the peroxisome and were by and We PEX11 proteins these the to with other we cells with the and and and and and or and a was with either or for and the were by and with the PEX11 proteins were by either we observed and in cells with were between and These are in with that the of PEX11 proteins by (12Schrader M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. Chem. 1998; 273: 29607-29614Abstract Full Text Full Text PDF PubMed Scopus (215) Google Scholar), that PEX11 be one of the proteins is to the that of interaction between PEX11 proteins, we DLP1 with were with and and and or and for in and to The were by and with was in of these and also to show evidence of we a yeast to for between these DLP1 and but this to show evidence for interaction of DLP1 are by of the DLP1 and has been that some of these may have activities in Y. S. J. Cell Biol. 1998; PubMed Scopus Google Scholar, T. Y. H. Y. T. M. J. Biol. Chem. 1998; 273: Full Text Full Text PDF PubMed Scopus (50) Google Scholar). We of the the of DLP1 peroxisome These of DLP1 as shown in with the form the one in in human a no effect on peroxisome abundance also no effect on peroxisome abundance and and DLP1 to peroxisome division and The mutants of peroxisome division the factors in peroxisome division were of the PEX11 of peroxisomal membrane The of PEX11 proteins with peroxisome abundance in the and overexpression of PEX11 is to peroxisome division and peroxisome abundance. However, PEX11 to proteins involved in other organelle formation to for PEX11 PEX11 overexpression induces peroxisome division, but loss of PEX11 peroxisome division and results in a reduction in peroxisome abundance, in mammalian and yeast cells (7Erdmann R. Blobel G. J. Cell Biol. 1995; 128: 509-523Crossref PubMed Scopus (230) Google Scholar, 8Marshall P. Krimkevich Y. Lark R. Dyer J. Veenhuis M. Goodman J. J. Cell Biol. 1995; 129: 345-355Crossref PubMed Scopus (173) Google Scholar, 14Li X. Baumgart E. Morrell J.C. Jimenez-Sanchez G. Valle D. Gould S.J. Mol. Cell. Biol. 2002; 22: 4358-4365Crossref PubMed Scopus (133) Google Scholar). is that PEX11 proteins play in peroxisome division than a conserved role in the of peroxisome division. In this we the by al. (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google that Vps1p, a dynamin-like protein of also plays a role in peroxisome division. many of Hoepfner et al. (19Hoepfner D. van den Berg M. Philippsen P. Tabak H.F. J. Cell Biol. 2001; PubMed Scopus Google many proteins required for peroxisome division in other these proteins with PEX11 these proteins to dynamin-like proteins peroxisome In this we have that DLP1 plays an essential role in peroxisome division in human cells and with suggest a model of peroxisome division in which of PEX11 to induce peroxisome division by recruiting DLP1 to We observed that there are two to PEX11-induced peroxisome division in human cells (12Schrader M. Reuber B.E. Morrell J.C. Jimenez-Sanchez G. Obie C. Stroh T. Valle D. Schroer T.A. Gould S.J. J. Biol. Chem. 1998; 273: 29607-29614Abstract Full Text Full Text PDF PubMed Scopus (215) Google Scholar, 17Li X. Gould S.J. J. Cell Biol. 2002; 156: 643-651Crossref PubMed Scopus (114) Google Scholar). The first phase involves peroxisome elongation and the segregation of PEX11 from other of the peroxisome The phase involves the division of these peroxisomes into small peroxisomes the We small of DLP1 on peroxisomes but overexpression of PEX11 the of peroxisome-associated Furthermore, that many of the elongated peroxisomes by PEX11 overexpression small that for These results suggest that PEX11 induces peroxisome division, at least in by recruiting DLP1 to peroxisome membranes. with this we that loss of DLP1 PEX11-mediated peroxisome division but PEX11-mediated elongation of peroxisomes or the formation of PEX11-enriched at the of the elongated be that PEX11 is to be the of DLP1 to membranes because loss of PEX11 in as a in peroxisome abundance as loss of DLP1 in human cells or loss of VPS1 in the to a model of peroxisome division in which PEX11 recruits DLP1 to peroxisome at of PEX11 we no evidence for between PEX11 and that are However, these results at least the that PEX11 to DLP1 have been in to membranes K. E. R. R. Smith G. EMBO J. PubMed Scopus Google Scholar, Y. P. B. Biol. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar, M. B. Mol. Cell. Biol. 1999; PubMed Scopus Google Scholar), and the of PEX11 peroxisomal membrane or the of of distinct which as of DLP1 the known of DLP1 with in a but important indirect mechanism for PEX11-mediated DLP1 is also to with of peroxisome division by other factors to the of DLP1 to for the of the a lines of evidence suggest that is the of DLP1 which is with peroxisomes is and by PEX11 DLP1 is on a small of peroxisomes and PEX11 overexpression is on elongated peroxisomes to division. we DLP1 on peroxisomes by to the of an peroxisomal membrane peroxisome division was indicating that DLP1 is an important in peroxisome division. transient interaction model for DLP1 is to that for in the formation of is to the membrane to formation and is Cell Biol. 2002; PubMed Scopus Google Scholar). for how DLP1 peroxisome division, little in the of into the function of dynamin-like has been to as a the of vesicles to form a which promotes of the membrane Cell. 1998; Full Text Full Text PDF PubMed Scopus Google Scholar, D. 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