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Armadillo Motifs Involved in Vesicular Transport

Armadillo (ARM) repeat proteins function in various cellular processes including vesicular transport and membrane tethering. They contain an imperfect repeating sequence motif that forms a conserved three-dimensional structure. Recently, structural and functional insight into tethering mediated by t...

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Detalles Bibliográficos
Autores principales: Striegl, Harald, Andrade-Navarro, Miguel A., Heinemann, Udo
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2813876/
https://www.ncbi.nlm.nih.gov/pubmed/20126549
http://dx.doi.org/10.1371/journal.pone.0008991
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author Striegl, Harald
Andrade-Navarro, Miguel A.
Heinemann, Udo
author_facet Striegl, Harald
Andrade-Navarro, Miguel A.
Heinemann, Udo
author_sort Striegl, Harald
collection PubMed
description Armadillo (ARM) repeat proteins function in various cellular processes including vesicular transport and membrane tethering. They contain an imperfect repeating sequence motif that forms a conserved three-dimensional structure. Recently, structural and functional insight into tethering mediated by the ARM-repeat protein p115 has been provided. Here we describe the p115 ARM-motifs for reasons of clarity and nomenclature and show that both sequence and structure are highly conserved among ARM-repeat proteins. We argue that there is no need to invoke repeat types other than ARM repeats for a proper description of the structure of the p115 globular head region. Additionally, we propose to define a new subfamily of ARM-like proteins and show lack of evidence that the ARM motifs found in p115 are present in other long coiled-coil tethering factors of the golgin family.
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spelling pubmed-28138762010-02-02 Armadillo Motifs Involved in Vesicular Transport Striegl, Harald Andrade-Navarro, Miguel A. Heinemann, Udo PLoS One Research Article Armadillo (ARM) repeat proteins function in various cellular processes including vesicular transport and membrane tethering. They contain an imperfect repeating sequence motif that forms a conserved three-dimensional structure. Recently, structural and functional insight into tethering mediated by the ARM-repeat protein p115 has been provided. Here we describe the p115 ARM-motifs for reasons of clarity and nomenclature and show that both sequence and structure are highly conserved among ARM-repeat proteins. We argue that there is no need to invoke repeat types other than ARM repeats for a proper description of the structure of the p115 globular head region. Additionally, we propose to define a new subfamily of ARM-like proteins and show lack of evidence that the ARM motifs found in p115 are present in other long coiled-coil tethering factors of the golgin family. Public Library of Science 2010-02-01 /pmc/articles/PMC2813876/ /pubmed/20126549 http://dx.doi.org/10.1371/journal.pone.0008991 Text en Striegl et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Striegl, Harald
Andrade-Navarro, Miguel A.
Heinemann, Udo
Armadillo Motifs Involved in Vesicular Transport
title Armadillo Motifs Involved in Vesicular Transport
title_full Armadillo Motifs Involved in Vesicular Transport
title_fullStr Armadillo Motifs Involved in Vesicular Transport
title_full_unstemmed Armadillo Motifs Involved in Vesicular Transport
title_short Armadillo Motifs Involved in Vesicular Transport
title_sort armadillo motifs involved in vesicular transport
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2813876/
https://www.ncbi.nlm.nih.gov/pubmed/20126549
http://dx.doi.org/10.1371/journal.pone.0008991
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