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Updated: Dec 26, 2025

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands
Published on: May 30, 2017
The interactome of the prostate-specific protein Anoctamin 7
Elina Kaikkonen1, Aliisa Takala1, Juha-Pekka Pursiheimo1
1Institute of Biomedicine, University of Turku, Turku, Finland.
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.
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