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
- Microtubule glutamylation is a dynamic post-translational modification that involves the addition of glutamate chains to tubulin, a process crucial for reshaping the biochemical interface of microtubules. This modification orchestrates an array of vital cellular functions, including cell division, neuronal development, and ciliary biology. We first delineate the molecular machinery by which glutamylation governs successive stages of cell division, encompassing centrosome-driven spindle assembly, spindle pole integrity maintenance, and the coordination of late mitotic events for faithful chromosome segregation and cytokinesis. We then examine how the dysregulation of this system drives oncogenesis. This includes loss-of-function perturbations, such as the downregulation of the tumor-suppressive enzyme TTLL11, which promotes chromosomal instability, as well as gain-of-function events involving oncogenic glutamylases like TTLL4, TTLL6, and TTLL12, which reprogram cytoskeletal dynamics to fuel proliferation, metastasis, and therapy resistance. Finally, we evaluate the resulting therapeutic landscape, discussing evolving strategies from metabolic intervention and direct enzyme inhibition to cutting-edge modalities like targeted protein degradation and synthetic biology for precision correction. Our analysis positions the glutamylation pathway not only as a fundamental regulator of cell division but also as a promising and multifaceted target for novel cancer therapeutics. - Source: PubMed
Publication date: 2026/08/20
Li KekeSun Shuang - The aim of the present study was to investigate the expression of tubulin-tyrosine ligase-like protein 12 (TTLL12) in oral squamous cell carcinoma (OSCC) and to explore its potential associations with clinicopathological characteristics and patient prognosis. - Source: PubMed
Publication date: 2026/05/27
Wang Yu-LuWang Yi-RunDong Lin-ShengLi Ya-Dong - 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