The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Legionella maintains host ubiquitin homeostasis by effectors with unique catalytic mechanisms
Open accessPreprint — published as 10.1038/s41467-024-50311-2 · Paper page
Abstract
The reversal of ubiquitination induced by members of the SidE effector family of Legionella pneumophila produces phosphoribosyl ubiquitin (PR-Ub) that is potentially detrimental to host cells. Here we show that the effector LnaB functions to transfer the AMP moiety from ATP to the phosphoryl moiety of PR-Ub to convert it into ADP-ribosylated ubiquitin (ADPR-Ub), which is further processed to ADP-ribose and functional ubiquitin by the (ADP-ribosyl)hydrolase MavL, thus maintaining ubiquitin homeostasis in infected cells. Upon being activated by Actin, LnaB also undergoes self-AMPylation on tyrosine residues. The activity of LnaB requires a motif consisting of Ser, His and Glu (S-HxxxE) present in a large family of toxins from diverse bacterial pathogens. Our study not only reveals intricate mechanisms for a pathogen to maintain ubiquitin homeostasis but also identifies a new family of enzymes capable of protein AMPylation, suggesting that this posttranslational modification is widely used in signaling during host-pathogen interactions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Metadata
- Authors
- Luo, Z.-Q., Fu, J., Li, S., Xian, W., Zhang, Z., Chen, T.-T., Liu, Y., Lu, Q., Ouyang, S., Das, C., Liu, X., Song, L., Guan, H., Li, C., Guan, Q., Wang, J., Li, J., Kang, L., Zheng, S.-R., & Cao, S.
- Affiliations
- Purdue University West Lafayette (US)
- First Hospital of Jilin University (CN)
- Peking University (CN)
- Fujian Normal University (CN)
- Fuzhou University (CN)
- Corresponding author
- Luo, Zhao-Qing
- Ouyang, Songying
- Liu, Xiaoyun
- Song, Lei
- ORCID
- Venue
- Nature Communications
- Published
- 2024-05-20
- Volume
- 15
- Issue
- 1
- Pages
- 5953-5953
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11251166
- OpenAlex
- W4400645073
- Cited by
- 34
- References
- 1
- Citations by year
- 2026: 13 · 2025: 12 · 2024: 9
- FWCI
- 10.10
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Foundation for the National Institutes of Health (R01AI127465, R01GM126296)
- National Natural Science Foundation of China (32171265, 31900879, 31900879 and 32171265, 82172287, 22174003, 32370185, 82225028, 82225028 and 82172287, 21974002, 32270185)
- Jilin University
- Fujian Normal University ((Z0210509))
- National Institutes of Health
- National Key Research and Development Program of China (2022YFA1304500, 2021YFC2301403)
- First Hospital of Jilin University
- National Institute of General Medical Sciences (R01GM126296)
- National Institute of Allergy and Infectious Diseases (R01AI127465)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Legionella and Acanthamoeba research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Legionella pneumophila, ubiquitin homeostasis, ADP-ribosylation, bacterial effector proteins, host-pathogen interaction
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
