Self-interaction of human Pex11pβ during peroxisomal growth and division.

Pex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies w...

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Autores principales:	Nina A Bonekamp, Sandra Grille, Maria Joao Cardoso, Monica Almeida, Miguel Aroso, Silvia Gomes, Ana Cristina Magalhaes, Daniela Ribeiro, Markus Islinger, Michael Schrader
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1d312833ac8346b3aa2ffa78f518cd43
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spelling	oai:doaj.org-article:1d312833ac8346b3aa2ffa78f518cd432021-11-18T08:02:29ZSelf-interaction of human Pex11pβ during peroxisomal growth and division.1932-620310.1371/journal.pone.0053424https://doaj.org/article/1d312833ac8346b3aa2ffa78f518cd432013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23308220/?tool=EBIhttps://doaj.org/toc/1932-6203Pex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies with an epitope-specific antibody and protease protection assays show that Pex11pβ is an integral membrane protein with two transmembrane domains flanking an internal region exposed to the peroxisomal matrix and N- and C-termini facing the cytosol. A glycine-rich internal region within Pex11pβ is dispensable for peroxisome membrane elongation and division. However, we demonstrate that an amphipathic helix (Helix 2) within the first N-terminal 40 amino acids is crucial for membrane elongation and self-interaction of Pex11pβ. Interestingly, we find that Pex11pβ self-interaction strongly depends on the detergent used for solubilization. We also show that N-terminal cysteines are not essential for membrane elongation, and that putative N-terminal phosphorylation sites are dispensable for Pex11pβ function. We propose that self-interaction of Pex11pβ regulates its membrane deforming activity in conjunction with membrane lipids.Nina A BonekampSandra GrilleMaria Joao CardosoMonica AlmeidaMiguel ArosoSilvia GomesAna Cristina MagalhaesDaniela RibeiroDaniela RibeiroMarkus IslingerMichael SchraderPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 1, p e53424 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Nina A Bonekamp Sandra Grille Maria Joao Cardoso Monica Almeida Miguel Aroso Silvia Gomes Ana Cristina Magalhaes Daniela Ribeiro Daniela Ribeiro Markus Islinger Michael Schrader Self-interaction of human Pex11pβ during peroxisomal growth and division.
description	Pex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies with an epitope-specific antibody and protease protection assays show that Pex11pβ is an integral membrane protein with two transmembrane domains flanking an internal region exposed to the peroxisomal matrix and N- and C-termini facing the cytosol. A glycine-rich internal region within Pex11pβ is dispensable for peroxisome membrane elongation and division. However, we demonstrate that an amphipathic helix (Helix 2) within the first N-terminal 40 amino acids is crucial for membrane elongation and self-interaction of Pex11pβ. Interestingly, we find that Pex11pβ self-interaction strongly depends on the detergent used for solubilization. We also show that N-terminal cysteines are not essential for membrane elongation, and that putative N-terminal phosphorylation sites are dispensable for Pex11pβ function. We propose that self-interaction of Pex11pβ regulates its membrane deforming activity in conjunction with membrane lipids.
format	article
author	Nina A Bonekamp Sandra Grille Maria Joao Cardoso Monica Almeida Miguel Aroso Silvia Gomes Ana Cristina Magalhaes Daniela Ribeiro Daniela Ribeiro Markus Islinger Michael Schrader
author_facet	Nina A Bonekamp Sandra Grille Maria Joao Cardoso Monica Almeida Miguel Aroso Silvia Gomes Ana Cristina Magalhaes Daniela Ribeiro Daniela Ribeiro Markus Islinger Michael Schrader
author_sort	Nina A Bonekamp
title	Self-interaction of human Pex11pβ during peroxisomal growth and division.
title_short	Self-interaction of human Pex11pβ during peroxisomal growth and division.
title_full	Self-interaction of human Pex11pβ during peroxisomal growth and division.
title_fullStr	Self-interaction of human Pex11pβ during peroxisomal growth and division.
title_full_unstemmed	Self-interaction of human Pex11pβ during peroxisomal growth and division.
title_sort	self-interaction of human pex11pβ during peroxisomal growth and division.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/1d312833ac8346b3aa2ffa78f518cd43
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Self-interaction of human Pex11pβ during peroxisomal growth and division.

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