Preprint Brief Report Version 1 Preserved in Portico This version is not peer-reviewed

Membrane Localization and Phosphorylation of Indoleamine 2,3-Dioxygenase 2 (IDO2) in A549 Human Lung Adenocarcinoma Cells: First Steps in Exploring Its Signaling Function

Chiara Suvieri
,
Francesca De Marchis
ORCID logo ,
Martina Mandarano
,
Sara Ambrosino
,
Sofia Rossini
ORCID logo ,
Giada Mondanelli
ORCID logo ,
Marco Gargaro
ORCID logo ,
Eleonora Panfili
,
Ciriana Orabona
ORCID logo ,
Maria Teresa Pallotta
ORCID logo ,
Maria Laura Belladonna
† ORCID logo ,
Claudia Volpi
*,† ORCID logo
†
These authors have contributed equally to this work and shared the last authorship
Version 1 : Received: 18 September 2023 / Approved: 19 September 2023 / Online: 19 September 2023 (04:21:41 CEST)

A peer-reviewed article of this Preprint also exists.

Suvieri, C.; De Marchis, F.; Mandarano, M.; Ambrosino, S.; Rossini, S.; Mondanelli, G.; Gargaro, M.; Panfili, E.; Orabona, C.; Pallotta, M.T.; Belladonna, M.L.; Volpi, C. Membrane Localization and Phosphorylation of Indoleamine 2,3-Dioxygenase 2 (IDO2) in A549 Human Lung Adenocarcinoma Cells: First Steps in Exploring Its Signaling Function. Int. J. Mol. Sci. 2023, 24, 16236. Suvieri, C.; De Marchis, F.; Mandarano, M.; Ambrosino, S.; Rossini, S.; Mondanelli, G.; Gargaro, M.; Panfili, E.; Orabona, C.; Pallotta, M.T.; Belladonna, M.L.; Volpi, C. Membrane Localization and Phosphorylation of Indoleamine 2,3-Dioxygenase 2 (IDO2) in A549 Human Lung Adenocarcinoma Cells: First Steps in Exploring Its Signaling Function. Int. J. Mol. Sci. 2023, 24, 16236.

Abstract

Indoleamine 2,3-dioxygenase 2 (IDO2) is a paralogue of IDO1, a tryptophan-degrading enzyme producing immunomodulatory molecules. However, the two proteins are unlikely to carry out the same functions. IDO2 shows little or no tryptophan catabolic activity and exerts contrasting immunomodulatory roles in a context-dependent manner, in both cancer and autoimmune diseases. The recently described potential non-enzymatic activity of IDO2 has suggested its possible involvement in alternative pathways resulting in either pro- or anti-inflammatory effects in different models. In a previous study on non-small cell lung cancer (NSCLC) tissues, we found that IDO2 expression, revealed at the plasma membrane level of tumor cells, was significantly associated with poor prognosis. In this study, the A549 human cell line, basally expressing IDO2, was used as an in vitro model of human lung adenocarcinoma to gain more insights on a possible alternative function of IDO2, different from the catalytic one. In these cells, immunocytochemistry and isopycnic sucrose gradient analyses confirmed the IDO2 protein localization in the cell membrane compartment, and immunoprecipitation of tyrosine-phosphorylated proteins revealed that IDO2 can be targeted by kinase activities. The different localization than the cytosolic one and the phosphorylation state are the first indications for the signaling function of IDO2, suggesting that the IDO2 non-enzymatic role in cancer cells is worthy of deeper understanding.

Keywords

IDO2; lung adenocarcinoma; A549; membrane localization; tyrosine-phosphorylation

Subject

Biology and Life Sciences, Life Sciences

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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