Myosin chaperones.
The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure-function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.
Research Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria.
Doris
D
Hellerschmied
Research Institute of Molecular Pathology, Dr. Bohrgasse 7, A-1030 Vienna, Austria. Electronic address: clausen@imp.univie.ac.at.
Tim
T
Clausen
D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D009218:Myosins / Q000737:chemistry / Q000378:metabolism*; D066329:Protein Aggregates; D017510:Protein Folding
D018832:Molecular Chaperones; D066329:Protein Aggregates; D009218:Myosins