ArticleJournal of cell science2022
Ca2+-dependent protein acyltransferase DHHC21 controls activation of CD4+ T cells.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.
- The role of palmitoylation modifications in the regulation of bone cell function, bone homeostasis, and osteoporosis.Bone & joint research · 2025Pooled it
- The role of protein palmitoylation in disease pathogenesis and therapeutic innovation.Annals of medicine · 2026Review
- Post‑translational modification‑governed immune states in cancer immunity: Biomarker implications for checkpoint competence, tumor visibility and immunotherapy resistance (Review).International journal of oncology · 2026Review
- DHHC21 is a STIM1 protein S-acyltransferase that modulates immune function in vivo.Journal of cell science · 2026Article
- zDHHC21 loss of function activates lung fibroblasts by regulating PTEN palmitoylation.American journal of respiratory cell and molecular biology · 2026Article
- Article
- Kv1.3 palmitoylation regulates spatial distribution and channel removal from the immunological synapse.Cellular and molecular life sciences : CMLS · 2026Article
- Palmitoylation-dependent regulation of innate and adaptive immunity: molecular insights and translational opportunities.Cellular & molecular biology letters · 2026Review
- DHHC21 is a STIM1 protein S-acyltransferase that modulates immune functionbioRxiv : the preprint server for biology · 2025Article
- ZDHHC21-driven S-palmitoylation of Themis regulates the function of T cells and maintains homeostatic balance.Cell communication and signaling : CCS · 2025Article
- ZDHHC5 Mediates Immune Dysregulation Driving Generalized Anxiety Disorder Risk.Brain and behavior · 2025Article
- Palmitic acid and palmitoylation in cancer: Understanding, insights, and challenges.Innovation (Cambridge (Mass.)) · 2025Review
- AP-1 activates KCNN4-mediated Ca2Cell biology and toxicology · 2024Article
- S-acylation of CaChronic diseases and translational medicine · 2024Review
- The anti-inflammatory role of zDHHC23 through the promotion of macrophage M2 polarization and macrophage necroptosis in large yellow croaker (Frontiers in immunology · 2024Article
- Morin, the PPARγ agonist, inhibits Th17 differentiation by limiting fatty acid synthesis in collagen-induced arthritis.Cell biology and toxicology · 2023Article
- Regulatory mechanisms controlling store-operated calcium entry.Frontiers in physiology · 2023Review
- S-acylation of Orai1 regulates store-operated Ca2+ entry.Journal of cell science · 2022Article
- Regulation of T cell function by protein S-acylation.Frontiers in physiology · 2022Review
- Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Despite the recognized significance of reversible protein lipidation (S-acylation) for T cell receptor signal transduction, the enzymatic control of this post-translational modification in T cells remains poorly understood. Here, we demonstrate that DHHC21 (also known as ZDHHC21), a member of the DHHC family of mammalian protein acyltransferases, mediates T cell receptor-induced S-acylation of proximal T cell signaling proteins. Using Zdhhc21dep mice, which express a functionally deficient version of DHHC21, we show that DHHC21 is a Ca2+/calmodulin-dependent enzyme critical for activation of naïve CD4+ T cells in response to T cell receptor stimulation. We find that disruption of the Ca2+/calmodulin-binding domain of DHHC21 does not affect thymic T cell development but prevents differentiation of peripheral CD4+ T cells into Th1, Th2 and Th17 effector T helper lineages. Our findings identify DHHC21 as an essential component of the T cell receptor signaling machinery and define a new role for protein acyltransferases in regulation of T cell-mediated immunity.
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What Socratic holds
Registered trials
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 Socratic graph.