Reevaluation of the role of Pex1 and dynamin-related proteins in peroxisome membrane biogenesis

Autor: Ewald H. Hettema, Paul C. Galvin, James M. Nuttall, Lakhan Ekal, Alison M. Motley

Publikováno v: The Journal of Cell Biology

Analysis of Pex1 and dynamin-related protein function indicates peroxisomes multiply mainly by growth and division in Saccharomyces cerevisiae, whereas no evidence was found for the previously proposed role for Pex1 in peroxisome formation by fusion

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::218c3a3318f19c60d42781453afef898
https://doi.org/10.1083/jcb.201412066

Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae

Autor: Alison M, Motley, James M, Nuttall, Ewald H, Hettema

Publikováno v: The EMBO Journal

Pexophagy, peroxysome autophagy, is regulated in Saccharomyces cerevisiae by Atg36 by direct binding to peroxysome regulator Pex3, Atg8 and Atg11 of the core autophagy machinery.
Peroxisomes undergo rapid, selective autophagic degradation (pexop

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::7714c06b7ff83f8bd9e435ce0b8de19d
http://europepmc.org/articles/PMC3395097

Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p

Autor: Alison M. Motley, Gemma P. Ward, Ewald H. Hettema

Publikováno v: Journal of Cell Science. 121:1633-1640

Yeast peroxisomes multiply by fission. Fission requires two dynamin-related proteins, Dnm1p and Vps1p. Using an in vivo fission assay, we show that Dnm1p-dependent peroxisome fission requires Fis1p, Caf4p and Mdv1p. Fluorescence microscopy of cells e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34a94b60e37a9ad218b60a9d8a6c432c
https://doi.org/10.1242/jcs.026344

Clathrin-mediated endocytosis in AP-2–depleted cells

Autor: Matthew N.J. Seaman, Margaret S. Robinson, Nicholas A. Bright, Alison M. Motley

Publikováno v: The Journal of Cell Biology

We have used RNA interference to knock down the AP-2 μ2 subunit and clathrin heavy chain to undetectable levels in HeLaM cells. Clathrin-coated pits associated with the plasma membrane were still present in the AP-2–depleted cells, but they were 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c20df60b16ed7bfe47d6fd775b351a6
https://doi.org/10.1083/jcb.200305145

Impaired neuronal migration and endochondral ossification in Pex7 knockout mice: a model for rhizomelic chondrodysplasia punctata

Autor: Ingrid Ploegaert, Myriam Baes, Mieke Dewerchin, Vincent Everts, Pedro Brites, Petra A. W. Mooyer, Philippe Evrard, Pierre Gressens, Luc Schoonjans, Hans R. Waterham, Alison M Motley, Ronald J.A. Wanders, Peter Carmeliet, Marinus Duran

Publikováno v: Human molecular genetics, 12(18), 2255-2267. Oxford University Press
Brites, P, Motley, A M, Gressens, P, Mooyer, P A W, Ploegaert, I, Everts, V, Evrard, P, Carmeliet, P, Dewerchin, M, Schoonjans, L, Duran, M, Waterham, H R, Wanders, R J A & Baes, M 2003, ' Impaired neuronal migration and endochondral ossification in Pex7 knockout mice: a model for rhizomelic chondrodysplasia punctata ', Human molecular genetics, vol. 12, pp. 2255-2267 . https://doi.org/10.1093/hmg/ddg236
Human Molecular Genetics, 12, 2255-2267. Oxford University Press
Human molecular genetics, 12, 2255-2267. Oxford University Press

Rhizomelic chondrodysplasia punctata is a human autosomal recessive disorder characterized by skeletal, eye and brain abnormalities. The disorder is caused by mutations in the PEX7 gene, which encodes the receptor for a class of peroxisomal matrix en

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86b1baca8ec8ae55319ef8471ac9aceb
https://dare.uva.nl/personal/pure/en/publications/impaired-neuronal-migration-and-endochondral-ossification-in-pex7-knockout-mice-a-model-for-rhizomelic-chondrodysplasia-punctata(ce613f2e-cd1b-41a9-b79a-60ff7949b2e9).html