Missense mutations in MYOT encoding the sarcomeric Z-disk protein myotilin cause three main myopathic phenotypes including proximal limb-girdle muscular dystrophy, spheroid body myopathy, and late-onset distal myopathy. We describe a family carrying a heterozygous MYOT deletion (Tyr4_His9del) that clinically was characterized by an early-adult onset distal muscle weakness and pathologically by a myofibrillar myopathy (MFM). Molecular modeling of the full-length myotilin protein revealed that the 4-YERPKH-9 amino acids are involved in local interactions within the N-terminal portion of myotilin. Injection of in vitro synthetized mutated human MYOT RNA or of plasmid carrying its cDNA sequence in zebrafish embryos led to muscle defects characterized by sarcomeric disorganization of muscle fibers and widening of the I-band, and severe motor impairments. We identify MYOT novel Tyr4_His9 deletion as the cause of an early-onset MFM with a distal myopathy phenotype and provide data supporting the importance of the amino acid sequence for the structural role of myotilin in the sarcomeric organization of myofibers.
A novel in-frame deletion in MYOT causes an early adult onset distal myopathy
	
	
	
		
		
		
		
		
	
	
	
	
	
	
	
	
		
		
		
		
		
			
			
			
		
		
		
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
						
							
							
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
			
			
				
				
					
					
					
					
						
							
						
						
					
				
				
				
				
				
				
				
				
				
				
				
			
			
		
		
		
		
	
Malatesta, Manuela;Vettori, Andrea;Giorgetti, Alejandro;Cisterna, Barbara;Marchetto, Giulia;Tonin, Paola;Vattemi, Gaetano
	
		
		
	
			2023-01-01
Abstract
Missense mutations in MYOT encoding the sarcomeric Z-disk protein myotilin cause three main myopathic phenotypes including proximal limb-girdle muscular dystrophy, spheroid body myopathy, and late-onset distal myopathy. We describe a family carrying a heterozygous MYOT deletion (Tyr4_His9del) that clinically was characterized by an early-adult onset distal muscle weakness and pathologically by a myofibrillar myopathy (MFM). Molecular modeling of the full-length myotilin protein revealed that the 4-YERPKH-9 amino acids are involved in local interactions within the N-terminal portion of myotilin. Injection of in vitro synthetized mutated human MYOT RNA or of plasmid carrying its cDNA sequence in zebrafish embryos led to muscle defects characterized by sarcomeric disorganization of muscle fibers and widening of the I-band, and severe motor impairments. We identify MYOT novel Tyr4_His9 deletion as the cause of an early-onset MFM with a distal myopathy phenotype and provide data supporting the importance of the amino acid sequence for the structural role of myotilin in the sarcomeric organization of myofibers.| File | Dimensione | Formato | |
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