Evidence map›Paper›PMID 20388704›Full record

ArticleThe Journal of biological chemistry2010

Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases.

Corinna Lau, Christian Dölle, Toni I Gossmann, Line Agledal, Marc Niere, Mathias Ziegler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 64 citations in OpenAlex.

  1. Review
  2. Peripheral Neuropathy in Metabolic Stress.International journal of molecular sciences · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. SARM1-Dependent Axon Degeneration: Nucleotide Signaling, Neurodegenerative Disorders, Toxicity, and Therapeutic Opportunities.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
  7. Article
  8. Article
  9. Inhibitors of NADInternational journal of molecular sciences · 2024
    Review
  10. Review
  11. Heliyon · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Location, Location, Location: Compartmentalization of NADTrends in biochemical sciences · 2020
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Corinna LauDepartment of Molecular Biology, University of Bergen, N-5008 Bergen, Norway.
Christian Dölle
Toni I Gossmann
Line Agledal
Marc Niere
Mathias Ziegler
University of Bergen · NOUniversity of Sussex · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several important signaling pathways require NAD as substrate, thereby leading to significant consumption of the molecule. Because NAD is also an essential redox carrier, its continuous resynthesis is vital. In higher eukaryotes, maintenance of compartmentalized NAD pools is critical, but so far rather little is known about the regulation and subcellular distribution of NAD biosynthetic enzymes. The key step in NAD biosynthesis is the formation of the dinucleotide by nicotinamide/nicotinic acid mononucleotide adenylyltransferases (NMNATs). The three human isoforms were localized to the nucleus, the Golgi complex, and mitochondria. Here, we show that their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity, consistent with their absence from NMNATs of lower organisms. We further demonstrate that the Golgi-associated NMNAT is palmitoylated at two adjacent cysteine residues of its isoform-specific domain and thereby anchored at the cytoplasmic surface, a potential mechanism to regulate the cytosolic NAD pool. Insertion of unique domains thus provides a yet unrecognized enzyme targeting mode, which has also been adapted to modulate subcellular NAD supply.

Indexed as

Cell NucleusCysteineCytosolEnergy MetabolismGolgi ApparatusHeLa CellsHumansMitochondriaModels, BiologicalNicotinamide-Nucleotide AdenylyltransferaseProtein IsoformsProtein Processing, Post-TranslationalProteinsProtein Structure, TertiarySignal TransductionCysteineNicotinamide-Nucleotide AdenylyltransferaseProtein IsoformsProteins

Identifiers

PMID20388704
PMCPMC2881809
OpenAlexW1640068223

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.