Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Kaikkonen, Elina, Takala, Aliisa, Pursiheimo, Juha-Pekka, Wahlström, Gudrun, Schleutker, Johanna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: IOS Press 2020
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
_version_ 1783548737964998656
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
work_keys_str_mv AT kaikkonenelina theinteractomeoftheprostatespecificproteinanoctamin7
AT takalaaliisa theinteractomeoftheprostatespecificproteinanoctamin7
AT pursiheimojuhapekka theinteractomeoftheprostatespecificproteinanoctamin7
AT wahlstromgudrun theinteractomeoftheprostatespecificproteinanoctamin7
AT schleutkerjohanna theinteractomeoftheprostatespecificproteinanoctamin7
AT kaikkonenelina interactomeoftheprostatespecificproteinanoctamin7
AT takalaaliisa interactomeoftheprostatespecificproteinanoctamin7
AT pursiheimojuhapekka interactomeoftheprostatespecificproteinanoctamin7
AT wahlstromgudrun interactomeoftheprostatespecificproteinanoctamin7
AT schleutkerjohanna interactomeoftheprostatespecificproteinanoctamin7