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AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization

SYSNO ASEP	0544110
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization
Author(s)	Černocká, Hana (BFU-R)_{RID, ORCID} Vońka, P. (CZ) Kasalová, Veronika (BFU-R)_ORCID Sommerová, L. (CZ) Vandová, V. (CZ) Hrstka, R. (CZ) Ostatná, Veronika (BFU-R)_{RID, ORCID}
Number of authors	7
Article number	107808
Source Title	Bioelectrochemistry. - : Elsevier - ISSN 1567-5394 Roč. 140, aug 2021 (2021)
Number of pages	9 s.
Publication form	Online - E
Language	eng - English
Country	CH - Switzerland
Keywords	protein disulfide-isomerase ; gradient 2 protein ; anterior gradient-2 ; hydrogen evolution ; agr2 ; polylysine ; peptides
Subject RIV	CE - Biochemistry
OECD category	Biochemistry and molecular biology
R&D Projects	GA18-18154S GA ČR - Czech Science Foundation (CSF)
Method of publishing	Limited access
Institutional support	BFU-R - RVO:68081707
UT WOS	000663599500012
EID SCOPUS	85103759317
DOI	10.1016/j.bioelechem.2021.107808
Annotation	In this paper we compare electrochemical behavior of two homolog proteins, namely anterior gradient 2 (AGR2) and anterior gradient 3 (AGR3), playing an important role in cancer cell biology. The slight variation in their protein structures has an impact on protein adsorption and orientation at charged surface and also enables AGR2 and AGR3 to form heterocomplexes. We confirm interaction between AGR2 and AGR3 (i) in vitro by immunochemical and constant current chronopotentiometric stripping (CPS) analysis and (ii) in vivo by bioluminescence resonance energy transfer (BRET) assay. Mutation of AGR2 in dimerization domain (E60A) prevents development of wild type AGR2 dimers and also negatively affects interaction with wild type AGR3 as shown by CPS analysis. Beside new information about AGR2 and AGR3 protein including their joint interaction, our work introduces possible applications of CPS in bioanalysis of protein complexes, including those relatively unstable, but important in the cancer research.
Workplace	Institute of Biophysics
Contact	Jana Poláková, polakova@ibp.cz, Tel.: 541 517 244
Year of Publishing	2022
Electronic address	https://www.sciencedirect.com/science/article/pii/S1567539421000712

Number of the records: 1