LMOD2

Last update 08 May 2025

Basic Info

Synonyms

C-LMOD, Cardiac leiomodin, Leiomodin

+ [3]

Introduction

Mediates nucleation of actin filaments and thereby promotes actin polymerization (PubMed:18403713, PubMed:25250574, PubMed:26370058, PubMed:26417072). Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:18403713).

100 Clinical Results associated with LMOD2

100 Translational Medicine associated with LMOD2

0 Patents (Medical) associated with LMOD2

Literatures (Medical) associated with LMOD2

07 Jul 2025·Journal of General Physiology

Prediction and biological significance of small changes in binding of leiomodin to tropomyosin

Article

Author: Kostyukova, Alla S. ; Sánchez Díaz, Eduardo ; Tolkatchev, Dmitri ; Starks, Nickolas ; Gregorio, Carol C. ; Novak, Stefanie ; Minakhina, Svetlana ; Smith, Garry E. ; Osegueda, Brayan

In cardiac muscle, regulation of actin polymerization at the thin filament pointed end is controlled by two structurally similar but functionally antagonistic proteins, leiomodin-2 and tropomodulin-1. Both proteins contain tropomyosin-binding site 1, which is essential for their recruitment to the pointed end. Using circular dichroism, we determined changes in melting temperatures (ΔTm) for complexes of tropomyosin and leiomodin-2 fragments containing several hypomorphic mutations, which moderately affect binding to tropomyosin. We ran molecular dynamics simulations for the complexes and calculated standard Gibbs free energies of binding, which we found to strongly correlate with the ΔTm. We found that the E34Q mutation in leiomodin-2 resulted in a decrease in the melting temperature of the complex of tropomyosin and leiomodin-2 fragments, indicating a decrease in the affinity of leiomodin-2 for tropomyosin. Although modest, this change in in vitro affinity made leiomodin-2 a weaker competitor for tropomyosin than tropomodulin-1 in cardiomyocytes. This mutation significantly reduced the ability of leiomodin-2 to displace tropomodulin-1 at thin filament pointed ends and affected the ability of leiomodin-2 to elongate thin filaments. Our results highlight the essential role of the tropomyosin-binding site in the dynamic equilibrium between tropomodulin-1 and leiomodin-2 at the pointed end of thin filaments. Our data also suggest the potential use of the correlation between ΔTm and the modeled standard Gibbs free energies of binding to predict changes in the stability of complexes between tropomyosin and leiomodin or tropomodulin isoforms.

01 Dec 2024·Stem Cell Research

Establishment of heterozygous LMOD2 knockout human embryonic stem cell line (ZZUNEUi022-A-1) using CRISPR/Cas9 system

Article

Author: Jian, Liguo ; Sai, Yifu ; Zhang, Hui ; Li, Jing ; Jiang, Youxu ; Li, Xiaowei ; Zhang, Chunjin ; Guo, Guangli ; Sai, Yipu ; Sun, Liqiang ; Li, En ; Zhang, Lihua ; Su, Haitao

Dilated Cardiomyopathy (DCM), a prevalent form of cardiomyopathy, is characterized by ventricular dilation and systolic dysfunction. Its etiology is intricate, encompassing multiple genetic and environmental elements. The LMOD2 (Leiomodin 2) gene has been demonstrated to be closely associated with the pathogenesis of DCM. In this study, a pure cell line was generated by knocking out the LMOD2 gene, and a DCM cell model was established through induced differentiation, thus providing a powerful experimental approach for further understanding the pathogenesis of DCM. It also provides a potential research orientation for the early diagnosis and individualized treatment of DCM.

01 Apr 2024·Journal of Genetics and Genomics

Characterizing structural variants based on graph-genotyping provides insights into pig domestication and local adaption

Article

Author: Li, Xin ; Zhao, Shuhong ; Li, Xinyun ; Fu, Chong ; Li, Changchun ; Liu, Quan ; Li, Mengxun ; Zheng, Zhuqing

Structural variants (SVs), such as deletions (DELs) and insertions (INSs), contribute substantially to pig genetic diversity and phenotypic variation. Using a library of SVs discovered from long-read primary assemblies and short-read sequenced genomes, we map pig genomic SVs with a graph-based method for re-genotyping SVs in 402 genomes. Our results demonstrate that those SVs harboring specific trait-associated genes may greatly shape pig domestication and local adaptation. Further characterization of SVs reveals that some population-stratified SVs may alter the transcription of genes by affecting regulatory elements. We identify that the genotypes of two DELs (296-bp DEL, chr7: 52,172,101-52,172,397; 278-bp DEL, chr18: 23,840,143-23,840,421) located in muscle-specific enhancers are associated with the expression of target genes related to meat quality (FSD2) and muscle fiber hypertrophy (LMOD2 and WASL) in pigs. Our results highlight the role of SVs in domestic porcine evolution, and the identified candidate functional genes and SVs are valuable resources for future genomic research and breeding programs in pigs.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

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.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

LMOD2

Basic Info

Related

Analysis