Evidence map›Paper›PMID 18606142›Full record

ArticleDevelopmental cell2008

Neuraminidase 1 is a negative regulator of lysosomal exocytosis.

Gouri Yogalingam, Erik J Bonten, Diantha van de Vlekkert, Huimin Hu, Simon Moshiach, Samuel A Connell, Alessandra d'Azzo

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 6% 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

100 citing papers in PubMed, 1 synthesis or guideline pooled it, 177 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. TFEB and MCOLN1 are important forFrontiers in cellular and infection microbiology · 2026
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  7. Article
  8. Article
  9. Article
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  11. Article
  12. Article
  13. Review
  14. Article
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  16. Review
  17. AAV-mediated gene therapy for sialidosis.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  18. Article
  19. Review
  20. Article

40 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Gouri YogalingamDepartment of Genetics and Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105-2794, USA.
Erik J Bonten
Diantha van de Vlekkert
Huimin Hu
Simon Moshiach
Samuel A Connell
Alessandra d'Azzo
St. Jude Children's Research Hospital · US

Funding

FUNCTIONAL/STRUCTURAL STUDIES OF MAMMALIAN NEURAMINIDASER01GM060950 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI D'AZZO, ALESSANDRA · 2000 to 2009
$2.9M
GM1 as apoptotic signal in neurodegenerative GM1-gangliosidosisR01DK052025 · NIDDK · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI D'AZZO, ALESSANDRA · 1997 to 2010
$1.8M
GRADUATE RESEARCH SEMINAR IN BIOINORGANIC CHEMISTRYR13GM060905 · NIGMS · GORDON RESEARCH CONFERENCES · PI NUNEZ, MEGAN ELIZABETH · 2000 to 2000
$2k
FUNCTIONAL ROLES AND MECHANISMS OF SNO-RNAS IN PRE-RRNA PROCESSINGZ01DK052025 · NIDDK · DIABETES, DIGESTIVE, KIDNEY DISEASES · PI PECULIS, BRENDA A · 1996 to 2003
–
Intramural NIH HHS Z01 DK052025NIDDK NIH HHS DK52025NIDDK NIH HHS R01 DK052025NIGMS NIH HHS GM60905NIGMS NIH HHS R01 GM060950
6 · The paper itself

Abstract

Lysosomal exocytosis is a Ca2+-regulated mechanism that involves proteins responsible for cytoskeletal attachment and fusion of lysosomes with the plasma membrane. However, whether luminal lysosomal enzymes contribute to this process remains unknown. Here we show that neuraminidase NEU1 negatively regulates lysosomal exocytosis in hematopoietic cells by processing the sialic acids on the lysosomal membrane protein LAMP-1. In macrophages from NEU1-deficient mice, a model of the disease sialidosis, and in patients' fibroblasts, oversialylated LAMP-1 enhances lysosomal exocytosis. Silencing of LAMP-1 reverts this phenotype by interfering with the docking of lysosomes at the plasma membrane. In neu1-/- mice the excessive exocytosis of serine proteases in the bone niche leads to inactivation of extracellular serpins, premature degradation of VCAM-1, and loss of bone marrow retention. Our findings uncover an unexpected mechanism influencing lysosomal exocytosis and argue that exacerbations of this process form the basis for certain genetic diseases.

Indexed as

ExocytosisGene Expression RegulationAnimalsBone Marrow CellsCell MembraneCells, CulturedDisease Models, AnimalFibroblastsHumansLysosomal-Associated Membrane Protein 1LysosomesMacrophagesMiceMice, KnockoutModels, BiologicalMucolipidosesLysosomal-Associated Membrane Protein 1NEU1 protein, humanNeu1 protein, mouseNeuraminidase

Identifiers

PMID18606142
PMCPMC2664108
OpenAlexW2041274762

What OpenQuestion holds

Textmetadata
LicenceTDM
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.