Cited by 632Sphingolipid Metabolism and SignalingLysosomal Storage Disorders ResearchCancer, Lipids, and Metabolism

Mammalian ceramide synthases

Open access
Levy, Michal, Futerman, Anthony H.·2010·IUBMB Life

Abstract

In mammals, ceramide, a key intermediate in sphingolipid metabolism and an important signaling molecule, is synthesized by a family of six ceramide synthases (CerS), each of which synthesizes ceramides with distinct acyl chain lengths. There are a number of common biochemical features between the CerS, such as their catalytic mechanism, and their structure and intracellular localization. Different CerS also display remarkable differences in their biological properties, with each of them playing distinct roles in processes as diverse as cancer and tumor suppression, in the response to chemotherapeutic drugs, in apoptosis, and in neurodegenerative diseases. © 2010 IUBMB IUBMB Life, 62(5): 347–356, 2010

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Crossref · 10.1002/iub.319

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  • Ceramides produced by ceramide synthases 1-6 (CerS1-6) are the central molecules in sphingolipid metabolism.

    “Produced by ceramide synthases 1–6 (CerS1–6), ceramides are the central molecules in sphingolipid metabolism (12, 13, 14).”
  • The ADAMs contain prodomain and metalloprotease domains; the fold of the metalloprotease is known, but not that of the prodomain, which has no homologs of known structure.

    “The ADAMs contain prodomain and metalloprotease domains; the fold of the metalloprotease is known (23, 24), but not that of the prodomain, which has no homologs of known structure.”

    From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [24]

    The Structural features section (page unavailable) describes ceramide synthase domains, not ADAMs. Searches for ADAM prodomain and metalloprotease folds found no passage addressing the claim in our copy. (LLM, conf=0.78)

    Experimental — accuracy not yet measured

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Authors
Levy, M., & Futerman, A. H.
Affiliations
Weizmann Institute of Science (IL)
Corresponding author
Futerman, Anthony H.
Venue
IUBMB Life
Publisher
Wiley
Published
2010-03-10
Volume
62
Issue
5
Pages
347-356
ISSN
  • 1521-6543 (ISSN-L)
  • 1521-6551
OpenAlex
W1989832969
Cited by
632
References
82
Citations by year
2026: 35 · 2025: 41 · 2024: 55 · 2023: 52 · 2022: 49 · 2021: 57 · 2020: 42 · 2019: 38 · 2018: 49 · 2017: 41 · 2016: 33 · 2015: 41 · 2014: 19 · 2013: 33 · 2012: 22
FWCI
2.25
Type
journal article
Language
en
Open access
Locations
  • IUBMB Life (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Minerva Foundation
  • Israel Science Foundation
  • National Institutes of Health
  • National Institute of General Medical Sciences (R01GM076217, GM 076217)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
  • Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Keywords
ceramide synthase, ceramide synthesis, sphingolipid metabolism, catalytic mechanism, enzyme structure, subcellular localization, cancer, tumor suppression, chemotherapy response, apoptosis, neurodegenerative diseases
MeSH terms
Animals, Humans, Membrane Proteins, Neoplasms, Sphingosine, Gene Expression Regulation, Enzymologic, Tumor Suppressor Proteins, Sphingosine N-Acyltransferase

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