NME3

Last update 23 Jan 2025

Basic Info

Synonyms

DR-nm23, NDK 3, NDP kinase 3

+ [6]

Introduction

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis.

100 Clinical Results associated with NME3

100 Translational Medicine associated with NME3

0 Patents (Medical) associated with NME3

Literatures (Medical) associated with NME3

20 Sep 2024·ACS Chemical Biology

Mitochondrial Probe for Glutathione Depletion Reveals NME3 Essentiality for Mitochondrial Redox Response

Article

Author: Kelley, Shana O. ; Chen, Kangfu ; Zhang, Yi Y. ; Dhavarasa, Piriththiv ; Sack, Tanja ; Cerrato, Carmine P. ; Cheng, Ashley P.

Maintenance of the mitochondrial thiol redox state is essential for cell survival. However, we lack a comprehensive understanding of the redox response to mitochondrial glutathione depletion. We developed a mitochondria-penetrating peptide, mtCDNB, to specifically deplete mitochondrial glutathione. A genome-wide CRISPR/Cas9 screen in tandem with mtCDNB treatment was employed to uncover regulators of the redox response to mitochondrial glutathione depletion. We identified nucleoside diphosphate kinase 3 (NME3) as a regulator of mitochondrial dynamics. We show that NME3 is recruited to the mitochondrial outer membrane when under redox stress. In the absence of NME3, there is impaired mitophagy, which leads to the accumulation of dysfunctional mitochondria. NME3 knockouts depleted of mitochondrial glutathione have increased mitochondrial ROS production, accumulate mtDNA lesions, and present a senescence-associated secretory phenotype. Our findings suggest a novel role for NME3 in selecting mitochondria for degradation through mitophagy under conditions of mitochondrial redox stress.

01 Jun 2024·Cancer and Metastasis Reviews

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

Review

Author: Lomada, Santosh ; Zollo, Massimo ; Wieland, Thomas ; Ferrucci, Veronica

AbstractWe 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.

01 Apr 2024·Poultry Science

Proteomic-metabolomic combination analysis reveals novel biomarkers of meat quality that differ between young and older ducks

Article

Author: Gu, Tiantian ; Xu, Wenwu ; Lu, Lizhi ; Duan, Mingcai ; Chen, Li ; Zeng, Tao ; Tian, Yong

In order to explore the difference and its underlying mechanism between young and older ducks, 60-day-old (D60) and 300-day-old (D300) of young ducks and 900-day-old ducks (D900) of older ducks were selected and studied. HE staining indicated that breast muscle fibers in the D900 group were more inseparable than D60 and D300 groups and the greater redness were showed in D300 and D900 groups. Quantitative proteomic analyses were conducted to further identify differences between young and older ducks that 61 proteins overlapped in the comparative analysis of the D900 vs. D60 and D900 vs. D300 groups. Furthermore, metabolomics analysis from the D900 group showed marked differences from the results of the D60 and D300 groups in 31 unique metabolites. In particular, lower guanosine, hypoxanthine, guanine, and doxefazepam levels indicated the increased nutritional value of older ducks. Integrated proteomics and metabolomics analysis showed that purine metabolism was specifically enriched, indicating that NME3, RRM2B, AMPD1, and AMPD3 might mainly affect meat from older ducks. In conclusion, our results indicated that meat from 900-day-old ducks possessed a unique biochemical signature that could provide candidate biomarkers to distinguish young ducks from older ducks.

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NME3

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