ReviewJournal of biomedical science2015
The HRASLS (PLA/AT) subfamily of enzymes.
Review in Journal of biomedical science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- PLAAT2 suppresses gastric cancer progression by facilitating cMyc ubiquitination and inhibiting MEK/ERK signaling.Cell death & disease · 2026Article
- Systematic identification of Salmonella T6SS effectors uncovers diverse new families and lipid-targeting activities.PLoS biology · 2026Article
- HRASLS2 promotes the growth and glycolysis of pancreatic cancer by enhancing the stability of ASPH.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- PLAAT2 facilitates the development of pancreatic cancer and serves as a predictor of resistance to chemotherapy.BMC cancer · 2025Article
- Deciphering context-specific Axitinib escape pathways via multi-omics and explainable machine learning.Journal of translational medicine · 2025Article
- Exploiting autophagy and related pathways: pioneering new horizons in cataract therapy.Apoptosis : an international journal on programmed cell death · 2025Review
- A lipid metabolism and lysosome-based risk signature for prognosis and immune response prediction in uterine corpus endometrial carcinoma.Frontiers in genetics · 2025Article
- Gene loss and relaxed selection ofProceedings. Biological sciences · 2024Article
- Phospholipid biosynthetic pathways and lipodystrophies: a novel syndrome due to PLAAT3 deficiency.Nature reviews. Endocrinology · 2024Article
- The endoplasmic reticulum stress-related genes and molecular typing predicts prognosis and reveals characterization of tumor immune microenvironment in lung squamous cell carcinoma.Discover oncology · 2024Article
- Malignant peritoneal mesotheliomas of rats induced by multiwalled carbon nanotubes and amosite asbestos: transcriptome and epigenetic profiles.Particle and fibre toxicology · 2024Article
- Gene loss and relaxed selection ofbioRxiv : the preprint server for biology · 2023Article
- Identification of key lipid metabolism-related genes in Alzheimer's disease.Lipids in health and disease · 2023Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- AUTOPHAGY IN THE EYE: FROM PHYSIOLOGY TO PATHOPHYSOLOGY.Autophagy reports · 2023Article
- Effects of Lipid Metabolism-Related Genes PTGIS and HRASLS on Phenotype, Prognosis, and Tumor Immunity in Lung Squamous Cell Carcinoma.Oxidative medicine and cellular longevity · 2023Article
- Phospholipase A and acyltransferase 4/retinoic acid receptor responder 3 at the intersection of tumor suppression and pathogen restriction.Frontiers in immunology · 2023Review
- Phospholipase A/acyltransferase 4 is a prognostic biomarker and correlated with immune infiltrates in pancreatic cancer.Heliyon · 2022Article
- PLAAT1 Exhibits Phosphatidylcholine:Monolysocardiolipin Transacylase Activity.International journal of molecular sciences · 2022Article
- Suppression of PI3K signaling is linked to autophagy activation and the spatiotemporal induction of the lens organelle free zone.Experimental cell research · 2022Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The H-RAS-like suppressor (HRASLS) subfamily consists of five enzymes (1-5) in humans and three (1, 3, and 5) in mice and rats that share sequence homology with lecithin:retinol acyltransferase (LRAT). All HRASLS family members possess in vitro phospholipid metabolizing abilities including phospholipase A1/2 (PLA1/2) activities and O-acyltransferase activities for the remodeling of glycerophospholipid acyl chains, as well as N-acyltransferase activities for the production of N-acylphosphatidylethanolamines. The in vivo biological activities of the HRASLS enzymes have not yet been fully investigated. Research to date indicates involvement of this subfamily in a wide array of biological processes and, as a consequence, these five enzymes have undergone extensive rediscovery and renaming within different fields of research. This review briefly describes the discovery of each of the HRASLS enzymes and their role in cancer, and discusses the biochemical function of each enzyme, as well as the biological role, if known. Gaps in current understanding are highlighted and suggestions for future research directions are discussed.
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