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The interactome of the prostate-specific protein Anoctamin 7
BACKGROUND: Elevated Anoctamin 7 (ANO7) expression is associated with poor survival in prostate cancer patients. OBJECTIVE: The aim was to discover proteins that interact with ANO7 to understand its functions and regulatory mechanisms. METHODS: The proximity-dependent biotin identification (BioID) m...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
IOS Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7306890/ https://www.ncbi.nlm.nih.gov/pubmed/32176628 http://dx.doi.org/10.3233/CBM-190993 |
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author | Kaikkonen, Elina Takala, Aliisa Pursiheimo, Juha-Pekka Wahlström, Gudrun Schleutker, Johanna |
author_facet | Kaikkonen, Elina Takala, Aliisa Pursiheimo, Juha-Pekka Wahlström, Gudrun Schleutker, Johanna |
author_sort | Kaikkonen, Elina |
collection | PubMed |
description | BACKGROUND: Elevated Anoctamin 7 (ANO7) expression is associated with poor survival in prostate cancer patients. OBJECTIVE: The aim was to discover proteins that interact with ANO7 to understand its functions and regulatory mechanisms. METHODS: The proximity-dependent biotin identification (BioID) method was utilized. ANO7 fused to biotin ligase was transiently transfected into LNCaP cells, and the biotinylated proteins were collected and analysed by mass spectrometry. Four identified proteins were stained with dual fluorescent immunostaining and visualized using Stimulated emission depletion microscopy (STED). RESULTS: After bioinformatic filtering steps, 64 potentially ANO7-interacting proteins were identified and analysed with the GO enrichment analysis tool. One of the most prominently enriched cellular components was cellular vesicle. Co-localization was showed for staphylococcal nuclease and tudor domain containing 1 (SND1), heat shock protein family A (Hsp70) member 1A (HSPA1A), adaptor related protein complex 2 subunit beta 1 (AP2B1) and coatomer protein complex subunit gamma 2 (COPG2). CONCLUSIONS: This is the first study in which ANO7 interacting proteins have been identified. Although further studies are needed, the findings reported here expand our understanding of the role and regulation of ANO7 in prostate cancer cells. Furthermore, these results are likely to introduce new targets for the novel cancer therapies. |
format | Online Article Text |
id | pubmed-7306890 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | IOS Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-73068902020-06-23 The interactome of the prostate-specific protein Anoctamin 7 Kaikkonen, Elina Takala, Aliisa Pursiheimo, Juha-Pekka Wahlström, Gudrun Schleutker, Johanna Cancer Biomark Research Article BACKGROUND: Elevated Anoctamin 7 (ANO7) expression is associated with poor survival in prostate cancer patients. OBJECTIVE: The aim was to discover proteins that interact with ANO7 to understand its functions and regulatory mechanisms. METHODS: The proximity-dependent biotin identification (BioID) method was utilized. ANO7 fused to biotin ligase was transiently transfected into LNCaP cells, and the biotinylated proteins were collected and analysed by mass spectrometry. Four identified proteins were stained with dual fluorescent immunostaining and visualized using Stimulated emission depletion microscopy (STED). RESULTS: After bioinformatic filtering steps, 64 potentially ANO7-interacting proteins were identified and analysed with the GO enrichment analysis tool. One of the most prominently enriched cellular components was cellular vesicle. Co-localization was showed for staphylococcal nuclease and tudor domain containing 1 (SND1), heat shock protein family A (Hsp70) member 1A (HSPA1A), adaptor related protein complex 2 subunit beta 1 (AP2B1) and coatomer protein complex subunit gamma 2 (COPG2). CONCLUSIONS: This is the first study in which ANO7 interacting proteins have been identified. Although further studies are needed, the findings reported here expand our understanding of the role and regulation of ANO7 in prostate cancer cells. Furthermore, these results are likely to introduce new targets for the novel cancer therapies. IOS Press 2020-04-30 /pmc/articles/PMC7306890/ /pubmed/32176628 http://dx.doi.org/10.3233/CBM-190993 Text en © 2020 – IOS Press and the authors. All rights reserved https://creativecommons.org/licenses/by-nc/4.0/ This article is published online with Open Access and distributed under the terms of the Creative Commons Attribution Non-Commercial License (CC BY-NC 4.0). |
spellingShingle | Research Article Kaikkonen, Elina Takala, Aliisa Pursiheimo, Juha-Pekka Wahlström, Gudrun Schleutker, Johanna The interactome of the prostate-specific protein Anoctamin 7 |
title | The interactome of the prostate-specific protein Anoctamin 7 |
title_full | The interactome of the prostate-specific protein Anoctamin 7 |
title_fullStr | The interactome of the prostate-specific protein Anoctamin 7 |
title_full_unstemmed | The interactome of the prostate-specific protein Anoctamin 7 |
title_short | The interactome of the prostate-specific protein Anoctamin 7 |
title_sort | interactome of the prostate-specific protein anoctamin 7 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7306890/ https://www.ncbi.nlm.nih.gov/pubmed/32176628 http://dx.doi.org/10.3233/CBM-190993 |
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