PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor

PEX5 acts as a cycling receptor for import of PTS1 proteins into peroxisomes and as a co-receptor for PEX7, the PTS2 receptor, but the mechanism of cargo unloading has remained obscure. Using recombinant protein domains we show PEX5 binding to the PEX14N-terminal domain (PEX14N) has no effect on the...

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Autores principales: Lanyon-Hogg, Thomas, Hooper, Jacob, Gunn, Sarah, Warriner, Stuart L., Baker, Alison
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4065332/
https://www.ncbi.nlm.nih.gov/pubmed/24879895
http://dx.doi.org/10.1016/j.febslet.2014.05.038
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author Lanyon-Hogg, Thomas
Hooper, Jacob
Gunn, Sarah
Warriner, Stuart L.
Baker, Alison
author_facet Lanyon-Hogg, Thomas
Hooper, Jacob
Gunn, Sarah
Warriner, Stuart L.
Baker, Alison
author_sort Lanyon-Hogg, Thomas
collection PubMed
description PEX5 acts as a cycling receptor for import of PTS1 proteins into peroxisomes and as a co-receptor for PEX7, the PTS2 receptor, but the mechanism of cargo unloading has remained obscure. Using recombinant protein domains we show PEX5 binding to the PEX14N-terminal domain (PEX14N) has no effect on the affinity of PEX5 for a PTS1 containing peptide. PEX5 can form a complex containing both recombinant PTS1 cargo and endogenous PEX7-thiolase simultaneously but isolation of the complex via the PEX14 construct resulted in an absence of thiolase, suggesting a possible role for PEX14 in the unloading of PTS2 cargos.
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spelling pubmed-40653322014-06-27 PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor Lanyon-Hogg, Thomas Hooper, Jacob Gunn, Sarah Warriner, Stuart L. Baker, Alison FEBS Lett Article PEX5 acts as a cycling receptor for import of PTS1 proteins into peroxisomes and as a co-receptor for PEX7, the PTS2 receptor, but the mechanism of cargo unloading has remained obscure. Using recombinant protein domains we show PEX5 binding to the PEX14N-terminal domain (PEX14N) has no effect on the affinity of PEX5 for a PTS1 containing peptide. PEX5 can form a complex containing both recombinant PTS1 cargo and endogenous PEX7-thiolase simultaneously but isolation of the complex via the PEX14 construct resulted in an absence of thiolase, suggesting a possible role for PEX14 in the unloading of PTS2 cargos. Elsevier Science B.V 2014-06-27 /pmc/articles/PMC4065332/ /pubmed/24879895 http://dx.doi.org/10.1016/j.febslet.2014.05.038 Text en © 2014 The Authors http://creativecommons.org/licenses/by/3.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Lanyon-Hogg, Thomas
Hooper, Jacob
Gunn, Sarah
Warriner, Stuart L.
Baker, Alison
PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title_full PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title_fullStr PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title_full_unstemmed PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title_short PEX14 binding to Arabidopsis PEX5 has differential effects on PTS1 and PTS2 cargo occupancy of the receptor
title_sort pex14 binding to arabidopsis pex5 has differential effects on pts1 and pts2 cargo occupancy of the receptor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4065332/
https://www.ncbi.nlm.nih.gov/pubmed/24879895
http://dx.doi.org/10.1016/j.febslet.2014.05.038
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