Cited by 79Cellular transport and secretionATP Synthase and ATPases ResearchProtein Kinase Regulation and GTPase Signaling

The advantage of channeling nucleotides for very processive functions

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Zala, Diana, Schlattner, Uwe, Desvignes, Thomas, Bobe, Julien, Roux, Aurélien, Chavrier, Philippe, Boissan, Mathieu·2017·F1000Research

Abstract

Nucleoside triphosphate (NTP)s, like ATP (adenosine 5’-triphosphate) and GTP (guanosine 5’-triphosphate), have long been considered sufficiently concentrated and diffusible to fuel all cellular ATPases (adenosine triphosphatases) and GTPases (guanosine triphosphatases) in an energetically healthy cell without becoming limiting for function. However, increasing evidence for the importance of local ATP and GTP pools, synthesised in close proximity to ATP- or GTP-consuming reactions, has fundamentally challenged our view of energy metabolism. It has become evident that cellular energy metabolism occurs in many specialised ‘microcompartments’, where energy in the form of NTPs is transferred preferentially from NTP-generating modules directly to NTP-consuming modules. Such energy channeling occurs when diffusion through the cytosol is limited, where these modules are physically close and, in particular, if the NTP-consuming reaction has a very high turnover, i.e . is very processive. Here, we summarise the evidence for these conclusions and describe new insights into the physiological importance and molecular mechanisms of energy channeling gained from recent studies. In particular, we describe the role of glycolytic enzymes for axonal vesicle transport and nucleoside diphosphate kinases for the functions of dynamins and dynamin-related GTPases.

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  • Because the cellular GTP:GDP ratio is about 10, RAS-GEFs catalyse GDP-to-GTP exchange in cells.

    “RAS-GEFs can promote the release of either GDP or GTP from RAS proteins in vitro; however, because the cellular GTP:GDP ratio is ~10 (refs.8,9), they catalyse GDP-to-GTP exchange in cells.”

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Research works printed but not linked: 1

  1. [23]Schlattner U Wallimann T: Metabolite channeling.In: Lennarz WJ, Lane MD, editors. Encyclopedia of Biological Chemistry.2nd ed. New York: Academic Press; 2013; 80– 5.

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Authors
Zala, D., Schlattner, U., Desvignes, T., Bobe, J., Roux, A., Chavrier, P., & Boissan, M.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Inserm (FR)
  • University of Oregon (US)
  • Laboratoire de Physiologie et Génomique des Poissons (FR)
  • University of Geneva (CH)
Corresponding author
  • Zala, Diana
  • Boissan, Mathieu
Venue
F1000Research
Published
2017-07-18
Volume
6
Pages
724
ISSN
2046-1402 (ISSN-L)
OpenAlex
W2616097232
Cited by
79
References
238
Citations by year
2026: 6 · 2025: 7 · 2024: 6 · 2023: 12 · 2022: 6 · 2021: 28 · 2020: 8 · 2019: 3 · 2018: 3
FWCI
0.45
Type
journal article
Language
en
Open access
Locations
  • F1000Research (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • HAL (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Fondation pour la Recherche Médicale (FRM DPM20121125557)
  • Groupement des Entreprises Françaises contre le Cancer (GEFLUC R16170DD/RAK16044DDA)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
energy channeling, nucleoside triphosphates, ATP, GTP, ATPase, GTPase, processive enzymes, microcompartments, energy metabolism, glycolytic enzymes, nucleoside diphosphate kinase, dynamin-related GTPase, dynamin

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