Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy.

Journal article

Previous work has shown that mutations in muscle LIM protein (MLP) can cause hypertrophic cardiomyopathy (HCM). In order to gain an insight into the molecular basis of the disease phenotype, we analysed the binding characteristics of wild-type MLP and of the (C58G) mutant MLP that causes hypertrophic cardiomyopathy. We show that MLP can form a ternary complex with two of its previously documented myofibrillar ligand proteins, N-RAP and alpha-actinin, which indicates the presence of distinct, ...

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Authors: Gehmlich, K; Geier, C; Osterziel, K; Van der Ven, P; Fürst, DO

• Journal: Cell and tissue research
• Volume: 317
• Issue: 2
• Pages: 129-136
• Publication date: 2004-08-01
• DOI: 10.1007/s00441-004-0873-y
• EISSN: 1432-0878
• ISSN: 0302-766X
• Language: English
• Keywords: Cardiomyopathy, Hypertrophic; Humans; Muscle Cells; Binding Sites; Muscle Proteins; Protein Binding; Point Mutation; Actinin; Amino Acid Substitution; Multiprotein Complexes; Zinc; LIM Domain Proteins; Protein Structure, Quaternary