Clinically, dilated cardiomyopathy (DCM) is associated with a high rate of mortality due to the inefficient pumping of the heart and presence of life-threatening arrhythmias. Mutations in a diverse group of genes result in DCM, with genetic mutations now being identified in up to 40% of all DCM patients. Due to this high mutagenic rate a much better understanding of the genetic pathologies associated with DCM is needed. Recently, the first human Lmod2 cardiomyopathy was discovered in a pediatric patient who presented with DCM at birth. Exome sequencing revealed a bi-allelic nonsense mutation in the LMOD2 gene which encodes the protein, Leiomodin 2 (Lmod2). It has previously been demonstrated that Leiomodin 2 (Lmod2) is a sarcomeric protein known to tightly regulate actin-thin filament lengths by acting as a nucleator of actin polymerization, resulting in thin filament elongation. Together with the sarcomeric protein Tropomodulin (Tmod), which serves to cap and therefore shorten actin-thin filaments, Lmod2 is able to precisely fine-tune actin-thin filament lengths in the sarcomere and thus control efficient cardiac muscle contraction. To better understand the consequences of this mutation on the structure and function of the heart we have generated patient-derived iPSC-CMs harboring the Lmod2 mutation and a CRISPR/Cas9 isogenic control line. Through the use of human iPSC-CMs we are examining the biochemical and functional consequences of this mutation with the overall goal of effectively translating a patient’s clinical genotype into human iPSC-CMs. By investigating the structural effects, calcium handling properties, and contractility alterations in mutated human iPSC-CMs, we hope to identify the pathological role and disease state that arise from this Lmod2 mutation. Together, these experiments will provide important information on Lmod2, an understudied sarcomeric protein, that is necessary for heart function.