**3.2. Desmin**

One other regulating mitochondria affinity to ADP and oxygen consumption through direct binding to VDAC is the muscle-specific intermediate filament protein, desmin. The function of desmin is to form a three-dimensional scaffold that interconnects the contractile apparatus to the nucleus, cellular organelles, and the sarcolemma [28]. Proximity of sarcoplasmic reticulum and mitochondria by desmin scaffold allows facilitation of direct protein and metabolite targeting to mitochondria [29–31]. Interaction of desmin with contact sites (VDAC, adenine nucleotide translocator (ANT) and mitochondrial contact site complex) affects mitochondrial permeability transition pore (mtPTP) behavior and respiratory function [32, 33]. Studies on mice have shown that desmin deficiency leads to development of skeletal and myocardial defects associated with a deteriorated structure and function of mitochondria [22, 34]. Mitochondrial abnormalities cause cardiomyocyte death and myocardial degeneration, accompanied by inflammation and fibrosis, resulting in dilated cardiomyopathy and heart failure [35–38]. The cardiac-specific small heat-shock protein, αB-crystallin, was proven to rescue desmin-deficient heart failure and maintain mitochondrial functions through inhibition of mtPTP. In addition, similarly as tubulin, desmin affects mitochondrial bioenergetics through interaction with VDAC and ATP synthase [39].
