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Taken into account that marked dystrophic changes and severe concomitant mitochondrial abnormalities were only present in soleus muscles of HOM mice, these findings strongly imply that expression of mutant desmin is more harmful for slow-twitch muscle fibers.

Analysis of longitudinal sections of gastrocnemius muscle derived from HET animals demonstrated that the mutant desmin is not incorporated into the cross-striated wild-type desmin cytoskeleton, but segregated into desmin-positive protein aggregates (Fig.  4b; Fig. S4e).

Our knock-in mouse strain represents the first physiological animal model for autosomal dominant and recessive human desminopathies, as the expression of the mutant desmin is controlled by the endogenous gene regulation sites.

The analysis of skeletal muscle tissue from 3- and 16-month-old HET R349P mice showed no overt myopathic alterations indicating that the observed expression level of R349P mutant desmin is not sufficient to induce progressive skeletal muscle damage in these mice.

The analysis of cardiac tissue derived from HOM R349P mice showed a highly abnormal desmin-staining pattern in which the mutant desmin is enriched at the level of intercalated discs as well as in small dotted protein aggregates in the sarcoplasm of individual cardiomyocytes (Fig. S5a).

Here, the amount of mutant desmin was in a range from hardly detectable up to 30%% as compared to the signal intensity wild-type desmin.

In HET mice, the relative quantity of mutant desmin was within a range of 20 50 % in both skeletal and cardiac muscle tissue.

Similar amounts of mutant desmin were also observed in Coomassie brilliant blue stained 2D-gels of skeletal and cardiac muscle tissue lysates (data not shown).

Importantly, the analysis of skeletal and cardiac muscle tissue from HET animals revealed that mutant desmin was not incorporated into the cross-striated, wild-type desmin cytoskeleton, but was segregated into subsarcolemmal and sarcoplasmic protein aggregates.

In man and mice, the mutant desmin was predominantly detected in protein aggregates in the subsarcolemmal region, and, to a lesser extent, in the sarcoplasm of skeletal muscle fibers.

Furthermore, comparison of the protein aggregation pathology in different muscle groups revealed that the level of mutant desmin was much more abundant in diseased soleus muscle than in gastrocnemius and quadriceps femoris muscles, which showed no myopathic alterations.