PRUNE1 and NME/NDPK family proteins influence energy metabolism and signaling in cancer metastases.

Energy metabolism Exopolyphosphatase Immune system NME family NMR structures Nucleoside diphosphate kinase NDPK PRUNE1 Tumor microenvironment

Journal

Cancer metastasis reviews
ISSN: 1573-7233
Titre abrégé: Cancer Metastasis Rev
Pays: Netherlands
ID NLM: 8605731

Informations de publication

Date de publication:
05 Jan 2024
Historique:
received: 10 10 2023
accepted: 19 12 2023
medline: 5 1 2024
pubmed: 5 1 2024
entrez: 5 1 2024
Statut: aheadofprint

Résumé

We describe here the molecular basis of the complex formation of PRUNE1 with the tumor metastasis suppressors NME1 and NME2, two isoforms appertaining to the nucleoside diphosphate kinase (NDPK) enzyme family, and how this complex regulates signaling the immune system and energy metabolism, thereby shaping the tumor microenvironment (TME). Disrupting the interaction between NME1/2 and PRUNE1, as suggested, holds the potential to be an excellent therapeutic target for the treatment of cancer and the inhibition of metastasis dissemination. Furthermore, we postulate an interaction and regulation of the other Class I NME proteins, NME3 and NME4 proteins, with PRUNE1 and discuss potential functions. Class I NME1-4 proteins are NTP/NDP transphosphorylases required for balancing the intracellular pools of nucleotide diphosphates and triphosphates. They regulate different cellular functions by interacting with a large variety of other proteins, and in cancer and metastasis processes, they can exert pro- and anti-oncogenic properties depending on the cellular context. In this review, we therefore additionally discuss general aspects of class1 NME and PRUNE1 molecular structures as well as their posttranslational modifications and subcellular localization. The current knowledge on the contributions of PRUNE1 as well as NME proteins to signaling cascades is summarized with a special regard to cancer and metastasis.

Identifiants

pubmed: 38180572
doi: 10.1007/s10555-023-10165-4
pii: 10.1007/s10555-023-10165-4
doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Informations de copyright

© 2024. The Author(s).

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Auteurs

Veronica Ferrucci (V)

Department of Molecular Medicine and Medical Biotechnology, DMMBM, University of Naples, Federico II, Via Pansini 5, 80131, Naples, Italy.
CEINGE Biotecnologie Avanzate "Franco Salvatore", Via Gaetano Salvatore 486, 80145, Naples, Italy.

Santosh Lomada (S)

Experimental Pharmacology Mannheim, European Center for Angioscience, Medical Faculty Mannheim, Heidelberg University, 68167, Mannheim, Germany.
DZHK, German Center for Cardiovascular Research, Partner Site Heidelberg/Mannheim, 68167, Mannheim, Germany.

Thomas Wieland (T)

Experimental Pharmacology Mannheim, European Center for Angioscience, Medical Faculty Mannheim, Heidelberg University, 68167, Mannheim, Germany. thomas.wieland@medma.uni-heidelberg.de.
DZHK, German Center for Cardiovascular Research, Partner Site Heidelberg/Mannheim, 68167, Mannheim, Germany. thomas.wieland@medma.uni-heidelberg.de.
Medical Faculty Mannheim, Ludolf Krehl-Str. 13-17, 68167, Mannheim, Germany. thomas.wieland@medma.uni-heidelberg.de.

Massimo Zollo (M)

Department of Molecular Medicine and Medical Biotechnology, DMMBM, University of Naples, Federico II, Via Pansini 5, 80131, Naples, Italy. massimo.zollo@unina.it.
CEINGE Biotecnologie Avanzate "Franco Salvatore", Via Gaetano Salvatore 486, 80145, Naples, Italy. massimo.zollo@unina.it.
DAI Medicina di Laboratorio e Trasfusionale, 'AOU' Federico II Policlinico, 80131, Naples, Italy. massimo.zollo@unina.it.

Classifications MeSH