AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization

0544110 - BFÚ 2022 RIV CH eng J - Článek v odborném periodiku
Černocká, Hana - Vońka, P. - Kasalová, Veronika - Sommerová, L. - Vandová, V. - Hrstka, R. - Ostatná, Veronika
AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization.
Bioelectrochemistry. Roč. 140, aug 2021 (2021), č. článku 107808. ISSN 1567-5394. E-ISSN 1878-562X
Grant CEP: GA ČR(CZ) GA18-18154S
Institucionální podpora: RVO:68081707
Klíčová slova: protein disulfide-isomerase * gradient 2 protein * anterior gradient-2 * hydrogen evolution * agr2 * polylysine * peptides
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 5.760, rok: 2021
Způsob publikování: Omezený přístup
https://www.sciencedirect.com/science/article/pii/S1567539421000712

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.
Trvalý link: http://hdl.handle.net/11104/0321163