Open AccessPex11pβ-mediated growth and division of mammalian peroxisomes follows a maturation pathway
Author(s) -
Hannah K. Delille,
Brigitte Agricola,
S. Guimarães,
Heike Borta,
Georg H. Lüers,
Marc Fransen,
Michael Schrader
Publication year - 2010
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.062109
Subject(s) - peroxisome , biology , microbiology and biotechnology , endoplasmic reticulum , organelle , fis1 , cell division , membrane protein , dynamin , biochemistry , membrane , endocytosis , gene , receptor , mitochondrial fusion , cell , mitochondrial dna
Peroxisomes are ubiquitous subcellular organelles, which multiply by growth and division but can also form de novo via the endoplasmic reticulum. Growth and division of peroxisomes in mammalian cells involves elongation, membrane constriction and final fission. Dynamin-like protein (DLP1/Drp1) and its membrane adaptor Fis1 function in the later stages of peroxisome division, whereas the membrane peroxin Pex11pβ appears to act early in the process. We have discovered that a Pex11pβ-YFPm fusion protein can be used as a specific tool to further dissect peroxisomal growth and division. Pex11pβ-YFPm inhibited peroxisomal segmentation and division, but resulted in the formation of pre-peroxisomal membrane structures composed of globular domains and tubular extensions. Peroxisomal matrix and membrane proteins were targeted to distinct regions of the peroxisomal structures. Pex11pβ-mediated membrane formation was initiated at pre-existing peroxisomes, indicating that growth and division follows a multistep maturation pathway and that formation of mammalian peroxisomes is more complex than simple division of a pre-existing organelle. The implications of these findings on the mechanisms of peroxisome formation and membrane deformation are discussed.