A Novel MAP3K7 Variant Causing Loss of Function Identified in a Family With Cardiospondylocarpofacial Syndrome: Functional Validation and Molecular Insights

在患有心脊椎腕面综合征的家族中发现了一种导致功能丧失的新型MAP3K7变异:功能验证和分子机制研究

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Abstract

Mitogen-activated protein kinase kinase kinase 7 (MAP3K7), also known as transforming growth factor-β-activated kinase 1 (TAK1), is a widely expressed kinase that plays a crucial role in various cellular processes variants in the MAP3K7 gene have been implicated in two distinct genetic disorders: frontometaphyseal dysplasia Type 2 (FMD2) and cardiofaciocutaneous syndrome (CSCF). To elucidate the consequences of the MAP3K7 variant, we investigated a Chinese family with CSCF harboring a novel heterozygous MAP3K7 variant and examined the genotype-phenotype correlation. Functional validation was performed using clinical evaluations, whole-exome sequencing (WES), and biochemical assays, including western blotting to assess TAK1 phosphorylation levels and downstream signaling pathways. Clinical data and genomic DNA were collected from the proband and family members. WES identified a novel heterozygous variant in MAP3K7 (NM_145331.3: c.149 T > C, p.Val50Ala) inherited from the affected mother. Sequence conservation analysis revealed that the Val50 residue is highly conserved among vertebrates and is critical for ATP binding. Protein 3D modeling predicted that the Val50Ala variant disrupts the kinase domain structure, potentially impairing TAK1 function. In vitro overexpression experiments in human embryonic kidney 293T (HEK293T) cells demonstrated that the Val50Ala variant significantly reduced TAK1 phosphorylation levels. Furthermore, this variant differentially affected downstream signaling molecules (p38, p65, and JNK) compared with variants causing FMD2. Notably, stimulation with transforming growth factor-β (TGF-β) partially restored the altered phosphorylation patterns, suggesting a potential compensatory mechanism. Our study provides novel insights into the molecular pathogenesis of MAP3K7 variants associated with CSCF and FMD2. We demonstrate that the p.Val50Ala variant impairs TAK1 kinase activity and differentially affects downstream signaling pathways. These findings highlight the distinct molecular fingerprints of MAP3K7 variants causing CSCF versus FMD2 and underscore the importance of considering MAP3K7 variants in the differential diagnosis of syndromic congenital cardiac defects, recurrent infections, and global developmental delays. Our results also suggest that TGF-β signaling may offer a potential therapeutic target for modulating the effects of MAP3K7 variants.

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