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PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner
PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding sur...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4454178/ https://www.ncbi.nlm.nih.gov/pubmed/25657323 http://dx.doi.org/10.1091/mbc.E14-10-1448 |
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author | Madasu, Yadaiah Yang, Changsong Boczkowska, Malgorzata Bethoney, Kelley A. Zwolak, Adam Rebowski, Grzegorz Svitkina, Tatyana Dominguez, Roberto |
author_facet | Madasu, Yadaiah Yang, Changsong Boczkowska, Malgorzata Bethoney, Kelley A. Zwolak, Adam Rebowski, Grzegorz Svitkina, Tatyana Dominguez, Roberto |
author_sort | Madasu, Yadaiah |
collection | PubMed |
description | PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding surfaces of the BAR and PDZ domains adjacent to each other on the concave side of the banana-shaped PICK1 dimer. In the model, the ACT of one subunit of the dimer interacts with the PDZ and BAR domains of the other subunit, possibly accounting for autoinhibition. Consistently, full-length PICK1 shows diffuse cytoplasmic localization, but it clusters on vesicle-like structures that colocalize with the trans-Golgi network marker TGN38 upon deletion of either the ACT or PDZ domain. This localization is driven by the BAR domain. Live-cell imaging further reveals that PICK1-associated vesicles undergo fast, nondirectional motility in an F-actin–dependent manner, but deleting the ACT dramatically reduces vesicle speed. Thus the ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2/3 complex. |
format | Online Article Text |
id | pubmed-4454178 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-44541782015-06-16 PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner Madasu, Yadaiah Yang, Changsong Boczkowska, Malgorzata Bethoney, Kelley A. Zwolak, Adam Rebowski, Grzegorz Svitkina, Tatyana Dominguez, Roberto Mol Biol Cell Articles PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding surfaces of the BAR and PDZ domains adjacent to each other on the concave side of the banana-shaped PICK1 dimer. In the model, the ACT of one subunit of the dimer interacts with the PDZ and BAR domains of the other subunit, possibly accounting for autoinhibition. Consistently, full-length PICK1 shows diffuse cytoplasmic localization, but it clusters on vesicle-like structures that colocalize with the trans-Golgi network marker TGN38 upon deletion of either the ACT or PDZ domain. This localization is driven by the BAR domain. Live-cell imaging further reveals that PICK1-associated vesicles undergo fast, nondirectional motility in an F-actin–dependent manner, but deleting the ACT dramatically reduces vesicle speed. Thus the ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2/3 complex. The American Society for Cell Biology 2015-04-01 /pmc/articles/PMC4454178/ /pubmed/25657323 http://dx.doi.org/10.1091/mbc.E14-10-1448 Text en © 2015 Madasu et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Madasu, Yadaiah Yang, Changsong Boczkowska, Malgorzata Bethoney, Kelley A. Zwolak, Adam Rebowski, Grzegorz Svitkina, Tatyana Dominguez, Roberto PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title | PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title_full | PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title_fullStr | PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title_full_unstemmed | PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title_short | PICK1 is implicated in organelle motility in an Arp2/3 complex–independent manner |
title_sort | pick1 is implicated in organelle motility in an arp2/3 complex–independent manner |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4454178/ https://www.ncbi.nlm.nih.gov/pubmed/25657323 http://dx.doi.org/10.1091/mbc.E14-10-1448 |
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