Ask about this productRelated genes to: TTLL12 antibody
- Gene:
- TTLL12 NIH gene
- Name:
- tubulin tyrosine ligase like 12
- Previous symbol:
- -
- Synonyms:
- KIAA0153
- Chromosome:
- 22q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-02
- Date modifiied:
- 2016-10-05
Related products to: TTLL12 antibody
Related articles to: TTLL12 antibody
- Tubulin tyrosine ligase-like enzyme-12 (TTLL-12), belonging to the TTLL family, holds a crucial position in posttranslational tubulin modifications implicated in cancer development, making it a potential target for anti-tumor therapy. However, the precise mechanisms of TTLL12 in HCC remain inadequately elucidated. In this study, we found markedly elevated expression of TTLL12 in HCC tissues compared to their adjacent normal counterparts, which is strongly linked to an unfavorable prognosis. Functional assays demonstrated that knockdown of TTLL12 significantly suppressed HCC cell proliferation, whereas overexpression of TTLL12 promoted oncogenic behaviors. In vivo models further confirmed that TTLL12 enhances tumor growth, as indicated by larger tumors in TTLL12-overexpressing cells compared to vector controls. Mechanistically, TTLL12 suppressed ubiquitin-proteasome-mediated degradation of eEF1A1 via competing with Bood POZ-containing gene type 2 (BPOZ-2), which typically recruits eEF1A1 to CULLIN (CUL3), and ultimately results in an enhancement of cancer cell proliferation. Our analyses underscore the oncogenic potential of TTLL12 in hepatocarcinogenesis by safeguarding eEF1A1 from BPOZ-2- mediated degradation, introducing a novel therapeutic target for combating HCC. - Source: PubMed
Publication date: 2026/04/21
Leng KaimingYang ZhenLiming YaoMeng NanfengXu YiLiao GuanqunHan MeiShi Guangjun - Esophageal adenocarcinoma (EAC), the dominant subtype of esophageal cancer in developed countries, is a growing health problem, characterized by poor patient prognosis and dismal survival due to ineffective screening tools and a lack of efficacious options targeting the interception or treatment of EAC. Despite molecular advances, molecular targeting of EAC remains elusive, suggesting the need for identifying alternative targets with improved prognostic and therapeutic value. Herein, we performed RNA-sequencing analysis in EAC and Barrett's Esophagus (BE) precursor lesions to identify isoform switching events significantly linked with all-cause and cancer-specific mortality. Patients were stratified based on histopathology alone or in combination with TP53 mutation status, the most commonly mutated gene in EAC. To gain mechanistic insight, we performed isoform-specific siRNA knockdown of two isoforms, TTLL12 and HM13, both linked to patient survival, and investigated mechanisms associated with isoform dysregulation and whether targeting specific isoforms in EAC acts synergistically to improve therapeutic potential. Isoform-specific knockdown of TTLL12 and HM13 significantly decreased the viability of two EAC cell lines, sensitized EAC cell lines to standard-of-care chemotherapy agents (paclitaxel and carboplatin) with synergy, and inhibited EAC cell migratory potential. Knockdown of the TTLL12 isoform led to activation of chaperone-mediated autophagy, which, in turn, decreased expression of CHK1 and TP53; whereas knockdown of the HM13 isoform activated the unfolded protein response and induced endoplasmic reticulum stress-induced autophagy and apoptosis. In addition, HM13 isoform knockdown increased the response to an anti-PD-L1 agent, avelumab, in EAC cells, suggesting a role for isoform switching in immunosuppression. Taken together, study results suggest that isoform switching may provide novel insight for the identification of prognostic markers and inform new potential therapeutic targets for EAC treatment or prevention. - Source: PubMed
Publication date: 2026/03/11
Zhang YunNtsiful David AIsrael RachelVandenburg BryceBarnett ShariRiethoven Jean-JackClarke Jennifer LLagisetty Kiran HLin JulesReddy Rishindra MChang Andrew COdell David DDiFeo AnalisaSartor Maureen AKresty Laura A - The majority of patients treated with immunotherapy as a standalone therapy experience little to no benefits. Tubulin tyrosine ligase 12 (TTLL12), as a member of the tubulin tyrosine ligase protein family, is associated with the prognosis of patients with cancer and implicated in regulating innate immunity. However, the role of TTLL12 in modulating antitumor immunity remains unclear. - Source: PubMed
Publication date: 2025/06/03
Chen Dong-WenCheng Yi-KanLi Pei-SiWu Xiao-JianHuang Xin-XinLong Jia-HuiXiong ZhizhongChen ChongYe Shu-BiaoLan Ping - What are the profiles of tubulin post-translational modifications (PTM) in the meiotic spindles of oocytes with different developmental competence: in-vivo matured MII oocytes (IVO) versus cumulus-free in-vitro matured germinal vesicles (IVM)? - Source: PubMed
Publication date: 2024/02/09
Karamtzioti ParaskeviFerrer-Vaquer AnnaBarragan MontserratVernos IsabelleVassena RitaTiscornia Gustavo - Rice plants are important food crops that are sensitive to cold stress. Microtubules (MTs) are highly associated with plant response to cold stress. The exogenous application of abscisic acid (ABA) can transiently induce the cold stability of microtubules. These phenotypes were accompanied by the transient increase in Phospholipase D (PLD) enzyme activity. The analysis of detyrosinated/tyrosinated α-tubulin by Western blot in the NtTUA3 line or in the NtTUA3+OsTTL line gave us such a conclusion that the effect of ABA on detyrosinated α-tubulin not only was regulated by ABA but also was dependent on the TTLL12 protein. The dual ABA and 1% n-butanol treatments had shown that ABA-induced detyrosinated α-tubulin in a manner distinct from the n-butanol pathway. Detecting the detyrosinated α-tubulin level after pre-treatment with pertussis toxin (PTX), a G-protein inhibitor, followed by ABA, as well as mastoparan (Mas7) treatment suggested that the effect of ABA on detyrosinated α-tubulin was dependent on PLD activity. - Source: PubMed
Publication date: 2024/12/31
Liu XuanRiemann MichaelNick Peter