Pex11p is required for peroxisome proliferation. This study demonstrates that the N-terminus of Pex11p forms an amphipathic helix that generates membrane curvature required for peroxisome fission

Anton

Campelo

Chris Williams

Dawson

Drin

Erdmann

Faber

Fagarasanu

Ford

Gallop

Gould

Guerra-Giraldez

Hatzakis

Hettema

Huang

Ida J van der Klei

Jan A K W Kiel

Kiel

Kobayashi

Krauss

Krikken

Kweon

Lamas-Maceiras

Lundmark

Marshall

Marten Veenhuis

Masuda

McMahon

Mukhopadhyay

Muller

Nagotu

Pettersen

Reynwar

Sambrook

Schumann

Shibata

Sprote

Takahashi

Thoms

van den Berg

van den Bosch

Vogel

Wriessnegger

Zimmerberg

Łukasz Opaliński

English

PubMed

Crossref

The EMBO Journal

Membrane curvature during peroxisome fission requires Pex11

Pex11 is a key player in peroxisome proliferation, but the molecular mechanisms of its function are still unknown. Here, we show that Pex11 contains a conserved sequence at the N-terminus that can adopt the structure of an amphipathic helix. Using Penicillium chrysogenum Pex11, we show that this amphipathic helix, termed Pex11-Amph, associates with liposomes in vitro. This interaction is especially evident when negatively charged liposomes are used with a phospholipid content resembling that of peroxisomal membranes. Binding of Pex11-Amph to negatively charged membrane vesicles resulted in strong tubulation. This tubulation of vesicles was also observed when the entire soluble N-terminal domain of Pex11 was used. Using mutant peptides, we demonstrate that maintaining the amphipathic properties of Pex11-Amph in conjunction with retaining its α-helical structure are crucial for its function. We show that the membrane remodelling capacity of the amphipathic helix in Pex11 is conserved from yeast to man. Finally, we demonstrate that mutations abolishing the membrane remodelling activity of the Pex11-Amph domain also hamper the function of full-length Pex11 in peroxisome fission in vivo.

Opaliński, Łukasz,

Kiel, Jan A.K.W.,

Williams, Chris,

Veenhuis, Marten,

Klei, Ida J. van der,

University of Groningen Digital Archive

Pex11 is a key player in peroxisome proliferation, but the molecular mechanisms of its function are still unknown. Here, we show that Pex11 contains a conserved sequence at the N-terminus that can adopt the structure of an amphipathic helix. Using Penicillium chrysogenum Pex11, we show that this amphipathic helix, termed Pex11-Amph, associates with liposomes in vitro. This interaction is especially evident when negatively charged liposomes are used with a phospholipid content resembling that of peroxisomal membranes. Binding of Pex11-Amph to negatively charged membrane vesicles resulted in strong tubulation. This tubulation of vesicles was also observed when the entire soluble N-terminal domain of Pex11 was used. Using mutant peptides, we demonstrate that maintaining the amphipathic properties of Pex11-Amph in conjunction with retaining its alpha-helical structure are crucial for its function. We show that the membrane remodelling capacity of the amphipathic helix in Pex11 is conserved from yeast to man. Finally, we demonstrate that mutations abolishing the membrane remodelling activity of the Pex11-Amph domain also hamper the function of full-length Pex11 in peroxisome fission in vivo. The EMBO Journal (2011) 30, 5-16. doi:10.1038/emboj.2010.299; Published online 26</p

Opalinski, Lukasz

Kiel, Jan A. K. W.

Williams, Chris

Veenhuis, Marten

van der Klei, Ida J.

ARTS repository - University of Groningen

Dissertations of the University of Groningen

Pex11 is a key player in peroxisome proliferation, but the molecular mechanisms of its function are still unknown. Here, we show that Pex11 contains a conserved sequence at the N-terminus that can adopt the structure of an amphipathic helix. Using Penicillium chrysogenum Pex11, we show that this amphipathic helix, termed Pex11-Amph, associates with liposomes in vitro. This interaction is especially evident when negatively charged liposomes are used with a phospholipid content resembling that of peroxisomal membranes. Binding of Pex11-Amph to negatively charged membrane vesicles resulted in strong tubulation. This tubulation of vesicles was also observed when the entire soluble N-terminal domain of Pex11 was used. Using mutant peptides, we demonstrate that maintaining the amphipathic properties of Pex11-Amph in conjunction with retaining its alpha-helical structure are crucial for its function. We show that the membrane remodelling capacity of the amphipathic helix in Pex11 is conserved from yeast to man. Finally, we demonstrate that mutations abolishing the membrane remodelling activity of the Pex11-Amph domain also hamper the function of full-length Pex11 in peroxisome fission in vivo. The EMBO Journal (2011) 30, 5-16. doi:10.1038/emboj.2010.299; Published online 2

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Proceedings - University of Groningen

University of Groningen

ARF- and coatomer-mediated peroxisomal vesiculation. Cell Biochem Biophys 32 (Spring): 27–36 Campelo

Biol 129: 345–355 Pex11-induced membrane curvature Ł Opalin ´ski et al &2011 European Molecular Biology Organization The

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Membrane curvature during peroxisome fission requires Pex11

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Crossref

University of Groningen Digital Archive

ARTS repository - University of Groningen

ARTS repository - University of Groningen

Dissertations of the University of Groningen

NARCIS

Proceedings - University of Groningen

University of Groningen

Proceedings - University of Groningen