CTNND1

Last update 08 May 2025

Basic Info

Synonyms

Cadherin-associated Src substrate, CAS, catenin delta 1

+ [10]

Introduction

Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476).

100 Clinical Results associated with CTNND1

100 Translational Medicine associated with CTNND1

0 Patents (Medical) associated with CTNND1

930

Literatures (Medical) associated with CTNND1

31 Dec 2025·Renal Failure

Combining mitochondrial proteomes and Mendelian randomization to identify novel therapeutic targets for diabetic nephropathy

Article

Author: Zhang, Jiaai ; Liu, Yang ; Zhou, Junan ; Zhou, Zhelun ; Wu, Rong ; Wang, Xiaoyi

Diabetic nephropathy (DN) is a common microvascular complication of diabetes. Mitochondrial dysfunction in the kidney caused by diabetes has previously been linked to the pathogenesis of DN. By mass spectrometry, we identified characteristic proteins of DN from the renal mitochondria in mouse model. To identify the core proteins among them, Mendelian randomization (MR) analysis, microarray data validation, and drug-target interaction analysis were employed. MR analysis found that 189 candidate targets had a causal link with DN risk factors (estimated glomerular filtration rate (eGFR), urinary albumin excretion, and serum creatinine). After systematic analysis, we validated that SLC25A16, CTNND1, C2CD2L, ALDH3A2, NEU1, APEH, CORO1A, NUDT19, and NDUFA4L2 are the core proteins with promising druggability in DN. This study suggests the feasibility of using MR analysis for DN drug target screening, and provides potential insights into mitochondrial dysfunction research, which may contribute to further DN pathogenesis exploration.

01 Apr 2025·Advanced Science

A Novel tRF, HCETSR, Derived From tRNA‐Glu/TTC, Inhibits HCC Malignancy by Regulating the SPBTN1‐catenin Complex Axis

Article

Author: Xu, Xiao ; Liu, Jian ; Ye, Qianwei ; Rui, Tao ; Pan, Yi ; Wu, Jiaping ; Chen, Cong ; Guo, Jufeng ; Xiang, Aizhai ; Zheng, Shusen ; Tang, Ning ; Zhu, Kangbei ; Zhang, Jing ; Mao, Zonglei

AbstracttRNA‐derived fragments (tRFs), a novel class of small non‐coding RNAs cleaved from transfer RNAs, have been implicated in tumor regulation. In this study, the role of a specific tRF, HCETSR is investigated, which is significantly downregulated in hepatocellular carcinoma (HCC) and correlates with advanced tumor burden and higher HCC mortality. Functional analyses revealed that HCETSR inhibits HCC malignancy and serves as an independent predictor of poor prognosis. Mechanistically, a novel SPTBN1/catenin complex axis regulated by HCETSR is identified. HCETSR binds to a critical domain of SPTBN1, disrupting its interaction with the catenin complex (comprising β‐catenin, α‐catenin, and P120‐catenin), and facilitates the transfer of the catenin complex from the cell membrane to the nucleus. Specifically, HCETSR decreases the proteasomal degradation of β‐catenin and inhibits the synthesis of nascent β‐catenin. Furthermore, HCETSR suppresses the transcriptional activity of LEF1 through P120‐catenin rather than α‐catenin, thereby reducing β‐catenin's influence on LEF1 activity. It is demonstrated that HCETSR is spliced from tRNA‐Glu/TTC. The biogenesis of HCETSR and tRNA‐Glu/TTC is regulated by the spliceosome and Dicer1. In conclusion, These findings suggest that HCETSR, derived from tRNA‐Glu/TTC, inhibits HCC malignancy via modulation of the SPTBN1/catenin axis and may represent a promising prognostic marker and therapeutic strategy for HCC.

01 Mar 2025·American Journal of Medical Genetics Part A

CTNND1‐Related Disorder: New Insight on Prenatal Phenotype

Article

Author: Natacci, F. ; Iascone, M. ; Hafdaoui, S. ; Marchetti, D. ; Silipigni, R. ; Runza, L. ; Cesaretti, C. ; Boito, S. ; Di Napoli, C. ; Accurti, V. ; Nicotra, V. ; Finelli, P. ; Conti, B.

ABSTRACTCTNND1 is a gene located in 11q12.1, encoding for p120 catenin, a protein involved in maintaining adherent junctions, regulating the epithelial–mesenchymal transition, and transcriptional signaling of different cellular pathways. Pathogenic variants in CTNND1 are classically associated with isolated cleft palate and Blefaro‐cheilo‐dontic syndrome, an autosomal dominant condition characterized by abnormalities of the eyelid. Considering different signs and symptoms associated first with Blefaro‐cheilo‐dontic syndrome and later specifically with CTNND1, Ahlaratani and colleagues proposed a wider developmental role for CTNND1 than previously described, associating a broader phenotypic spectrum. This report describes a prenatal case in which a CTNND1 pathogenic variant and reverse phenotyping allowed a diagnosis of Blefaro‐cheilo‐dontic syndrome associated with characteristics never related to Blefaro‐cheilo‐dontic syndrome or CTNND1, such as hydrocephalus. This report is the first detailed fetal case of Blefaro‐cheilo‐dontic syndrome, and the new feature reported is consistent with CTNND1 developmental role and may add new insights into the phenotype spectrum that is being defined.

Analysis

Perform a panoramic analysis of this field.

view full example data

Hiro LS Researcher

The AI Search Engine Built to Accelerate Biopharma Decisions

Search across billion-scale life sciences data to uncover signals, validate evidence, and act with confidence.

Ask any biopharma research question→

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, Patsnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Discover Synapse Data Servers

Synapse data is now integrated into the PatSnap LS Model Context Protocol (MCP) service. Customize your LLM agent now using our MCP server!

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis