title: [Intermediate-filament-associated diseases].
abstract: Intracellular protein filaments intermediate in size between actin filaments and           microtubules are composed of a variety of tissue specific proteins. The sequence           conservation of the coiled-coil alpha-helical structure responsible for polymerization           into individual 10 nm filaments defines a large gene family. Intermediate filaments (IFs)           include the nuclear lamins, which are universal in Metazoans, and the cytoplasmic           intermediate filaments, which are more varied and form cell type specific networks in           animal cells. IFs all share a common tripartite structure consisting of a highly conserved           central helical rod domain and variable N-head and C-tail domains. In contrast to actin           and tubulin, IFs do not require nucleoside triphosphates such as ATP or GTP for           polymerization but they self assemble. According to sequences, the IFs proteins are           grouped into seven classes, including five cytoplasmic, one nuclear and one sub-cortical           localizations. The search for functions of IFs has led to discoveries of roles in the           skin, heart, muscle, liver and brain, in premature aging and of involvement in several           degenerative disorders. Mutations in IFs cause or predispose to more than 80 human           tissue-specific diseases. Mouse models and gene invalidation have been extremely helpful           in eliciting IF role in physiopathology. Besides mechanical role in cell plasticity and           stress absorbers, IF functions are related to the capacity to interact with signaling           molecules and cell kinases, controlling gene regulatory networks. The reviews herein           include a historical perspective about IFs, describe how mutations affect IF structure and           assembly properties in desminopathies, inclusion formation in the neurodegenerative           Alexander disease, and how they induce multiple disorders in laminopathies.
authors: Génétique et Physiopathologie des Tissus Muscualaires, Université Pierre et Marie Curie, Paris Cedex, France. denise.paulin@upmc.fr
authors: Denise
authors: D
authors: Paulin
authors: Nicolas
authors: N
authors: Diguet
authors: Zhigang
authors: Z
authors: Xue
authors: Zhenlin
authors: Z
authors: Li
mesh_terms: D000818:Animals; D004195:Disease Models, Animal; D030342:Genetic Diseases, Inborn / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D006801:Humans; D007381:Intermediate Filament Proteins / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000502:physiology*; D007382:Intermediate Filaments / Q000502:physiology / Q000648:ultrastructure; D051379:Mice; D005810:Multigene Family; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000502:physiology; D019636:Neurodegenerative Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D007381:Intermediate Filament Proteins; D009419:Nerve Tissue Proteins