Ask about this productRelated genes to: Zdhhc11 antibody
- Gene:
- ZDHHC11 NIH gene
- Name:
- zinc finger DHHC-type containing 11
- Previous symbol:
- -
- Synonyms:
- ZNF399, FLJ13153
- Chromosome:
- 5p15.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-28
- Date modifiied:
- 2016-10-05
Related products to: Zdhhc11 antibody
Related articles to: Zdhhc11 antibody
- First-line treatment for gastric cancer (GC) includes PD-1 blockade with chemotherapy, but resistance challenges treatment success. We identify Streptococcus anginosus (SA) as a tumor-resident oncobacterium driving GC progression and immune evasion. SA is enriched in GC patient tumors and drives tumor growth in mice. SA extracellular vesicles (saEVs) translocate the bacterial chromatin remodeler saSNF2 into host cells. saSNF2 partners with host transcription factor TEAD1-through its ATPase activity and participation in BRG1/BRM-associated factor (BAF) complex assembly-to activate oncogenic transcription. This transkingdom interaction upregulates the palmitoyltransferase ZDHHC11, which stabilizes PD-L1 via palmitoylation to establish an immunosuppressive niche, while amplifying other TEAD1 target genes to fuel tumor progression. saEVs promote tumor growth and limit CD8 T cell infiltration in vivo. Pharmacological inhibition of ZDHHC11 reverses immune evasion and synergizes with anti-PD-1 checkpoint blockade. These findings establish SA as a multifaceted driver of GC and highlight the saSNF2-ZDHHC11 axis as a target to potentiate immunotherapy. - Source: PubMed
Publication date: 2026/09/07
Xie XiaoshanWei YueZheng JiayingZheng ZhikaiChen XijieWang JiaruiMa NingHuang XiaolingZhang PengZhang BoyuCai HanyongMa LiXiao LishiLiu QingxinWang WenyuNomura SachiyoChen ShiMeng XiangqiLee Mong-Hong - Lung cancer remains the most common cause of cancer-related mortality worldwide. The transforming growth factor-beta 1 (TGF-β1) pathway promotes epithelial-mesenchymal transition (EMT), invasion, and metastasis in advanced disease via mothers against decapentaplegic homolog 2 (Smad2) and Smad3. This study investigated how post-translational modifications regulate TGF-β1-Smad signaling. - Source: PubMed
Publication date: 2026/08/10
Li YulongZhou YuZhao PengShi MinWang ZhiyanZhang ZhijianQu Geping - Protein S-palmitoylation is a reversible lipid post-translational modification that dynamically controls protein localization, trafficking, receptor microdomain organization, autophagy and metabolic signalling. In osteoarticular tissues, this modification provides a plausible biochemical mechanism through which osteoclasts, osteoblast-lineage cells, osteocytes, chondrocytes, synoviocytes and skeletal-muscle cells integrate inflammatory, mechanical and metabolic cues. This review synthesizes current evidence linking S-palmitoylation and depalmitoylation to osteoarticular cell signalling and metabolic adaptation. We focus on experimentally supported mechanisms, including ZDHHC-mediated palmitoylation; depalmitoylation by APT, ABHD and PPT enzymes; palmitoylation-sensitive osteoclast differentiation; inflammatory priming of macrophage-derived osteoclast precursors; BMP/SMAD and organelle-contact-site signalling in osteoblast-lineage cells; ZDHHC11-dependent chondrocyte protection; ZDHHC4-mediated palmitoylation of CCDC50 followed by autophagic clearance of MAP2K4/MKK4; inflammasome regulation; CD36-associated lipid uptake; and palmitoylation-dependent transporter localization and turnover. We distinguish direct skeletal and joint evidence from mechanistic analogues derived from immune, neural, metabolic and cancer systems. We also clarify the distinction between reversible cysteine S-palmitoylation, broader S-acylation and other lipid modifications. Major barriers include incomplete definition of enzyme and substrate relationships, false-positive risk in palmitoyl-proteomic workflows, limited temporal resolution, insufficient validation in primary human tissues, uncertain tissue specificity and the off-target effects of non-selective palmitoylation inhibitors. A cell-biochemistry-centred view of the dynamic balance between palmitoylation and depalmitoylation may clarify how lipid modification regulates osteoarticular cell function and may help prioritize experimentally testable, substrate-specific mechanisms for future validation in osteoarthritis, osteoporosis and inflammatory joint disease. - Source: PubMed
Publication date: 2026/07/20
Huang XinqiWei XinpengTao YunHuang ZhimaoZhao ZhiheCen Xiao - Organophosphate esters (OPEs) are widely used flame retardants and plasticizers prevalent in indoor air, dust, and water. Studies suggest prenatal OPE exposure is linked to adverse maternal and infant outcomes, but the biological mechanisms remain unclear. - Source: PubMed
Publication date: 2026/07/03
Tang WanyiFoley HelenYang XiaoranMohazzab-Hosseinian SahraYang TingyuHernandez-Castro IxelKannan KurunthachalamXiang YijinMi HuaiyuWiemels JosephLewinger Juan PabloSiegmund KimberlyBastain TheresaBreton CarrieShu Chang - Palmitoylation is a key post-translational modification regulating viral replication, yet its regulatory mechanism in Dengue virus (DENV) infection remains elusive. This study aimed to elucidate the underlying regulatory function of palmitoylation and zinc finger Asp-His-His-Cys (ZDHHC) proteins in DENV replication and identify palmitoylated DENV proteins. We explored the function of palmitoylation in DENV replication using the palmitoylation inhibitor 2-bromopalmitate (2BP) and enhancer palmitic acid (PA), combined with qRT-PCR, western blot, confocal immunofluorescence microscopy, co-immunoprecipitation, and acyl-biotin exchange (ABE) assays. We found that 2BP promoted DENV replication, while PA inhibited it. Further analyses showed that 2BP and PA exerted no significant effects on DENV adsorption, internalization, or the interactions between E protein and the structural proteins prM/C that are essential for viral assembly. ABE assays verified that the DENV E protein is palmitoylated, with no such modification detected in prM and C proteins. Mass spectrometry and site-directed mutagenesis further revealed that the DENV E protein is palmitoylated at three cysteine residues: Cys74, Cys302, and Cys333. ZDHHC11, a characterized regulator of Zika virus E protein palmitoylation, directly interacted with DENV E protein and catalyzed its palmitoylation. Functionally, knockdown of ZDHHC11 enhanced DENV replication, while overexpression suppressed it. These findings deepen our understanding of flavivirus-host interaction mechanisms and provide a theoretical basis for the development of broad-spectrum anti-flavivirus therapies. - Source: PubMed
Publication date: 2026/05/03
Lai MingshuangZhang LexinLai RongjiDu QinLi ShilinLiu JinshengHe BaorenLi BinChen Limin