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  • 1
    Keywords: BIOLOGY ; ARCHITECTURE ; cytoskeleton ; PROTEIN ; CELL ; MICROSCOPY ; intermediate filament ; AMINO-ACID-SEQUENCE ; CROSS-LINKING ; review ; DESMIN ; ROD DOMAIN ; HUMAN VIMENTIN ; KERATIN FILAMENTS ; RAY SOLUTION SCATTERING ; SWITZERLAND ; COILED-COIL
    Type of Publication: Book chapter
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  • 2
    Keywords: CELL ; Germany ; human ; DISEASE ; DISEASES ; DISTINCT ; GENE ; PROTEIN ; PROTEINS ; INTERMEDIATE-SIZED FILAMENTS ; IMPACT ; BIOLOGY ; NUMBER ; MUTATION ; MUTATIONS ; US ; cytoskeleton ; intermediate filaments ; vimentin ; DE-NOVO ; ALPHA-B-CRYSTALLIN ; MICE LACKING DESMIN ; HUMAN-DISEASE ; ARCHITECTURE ; intermediate filament ; CHICKEN SKELETAL-MUSCLE ; desmin-related myopathy ; desminopathy ; filament assembly ; HEAD DOMAIN ; IMMUNOCYTOCHEMICAL ANALYSIS ; MYOFIBRILLAR MYOPATHY ; RESTRICTIVE CARDIOMYOPATHY ; VERTEBRATE SMOOTH-MUSCLE
    Abstract: Desmin, the major intermediate filament (IF) protein of muscle, is evolutionarily highly conserved from shark to man. Recently, an increasing number of mutations of the desmin gene has been described to be associated with human diseases such as certain skeletal and cardiac myopathies. These diseases are histologically characterised by intracellular aggregates containing desmin and various associated proteins. Although there is progress regarding our knowledge on the cellular function of desmin within the cytoskeleton, the impact of each distinct mutation is currently not understood at all. In order to get insight into how such mutations affect filament assembly and their integration into the cytoskeleton we need to establish IF structure at atomic detail. Recent progress in determining the dimer structure of the desmin-related IF-protein vimentin allows us to assess how such mutations may affect desmin filament architecture. (C) 2004 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 15477095
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  • 3
    Keywords: CELLS ; IN-VITRO ; CELL ; human ; MICROSCOPY ; MODEL ; MODELS ; PATHWAY ; VITRO ; DISEASE ; DISTINCT ; PROTEIN ; PROTEINS ; mechanisms ; DYNAMICS ; polymorphism ; OLIGOMERS ; cytoskeleton ; intermediate filaments ; INTERMEDIATE-FILAMENTS ; vimentin ; REVEALS ; DIMER ; electron microscopy ; intermediate filament ; ELECTRON-MICROSCOPY ; assembly ; PH ; HUMAN VIMENTIN ; analytical ultracentrifugation ; KERATIN FILAMENTS ; BIOLOGICAL MACROMOLECULES ; DIMERS ; AXES ; ADJACENT ; FILAMENTS ; 3D structure
    Abstract: intermediate filaments (IF's), along with microtubules, microfilaments, and associated cross-bridging proteins, constitute the cytoskeleton of metazoan cells. While crystallographic data on the dimer representing the elementary IF "building block" have recently become available, little structural detail is known about both the mature IF architecture and its assembly pathway. Here, we have applied solution small-angle x-ray scattering to investigate the in vitro assembly of a 53-kDa human IF protein vimentin at pH 8.4 by systematically varying the ionic strength conditions, and complemented these experiments by electron microscopy and analytical ultracentrifugation. While a vimentin solution in 5 mM Tris(.)HCl (pH 8.4) contains predominantly tetramers, addition of 20 mM NaCl induces further lateral assembly evidenced by the shift of the sedimentation coeficient and yields a distinct octameric intermediate. Four octamers eventually associate into unit-length filaments (ULFs) that anneal longitudinally. Based on the small-angle x-ray scattering experiments supplemented by crystallographic data and additional structural constraints, 3D molecular models of the vimentin tetramer, octamer, and ULF were constructed. Within each of the three oligomers, the adjacent dimers are aligned exclusively in an approximately half-staggered antiparallel A(11) mode with a distance of 3.2-3.4 nm between their axes. The ULF appears to be a dynamic and a relatively loosely packed structure with a roughly even mass distribution over its cross-section
    Type of Publication: Journal article published
    PubMed ID: 17050693
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  • 4
    Keywords: CELLS ; IN-VITRO ; CELL ; COMBINATION ; PROTEIN ; PROTEINS ; DIFFERENTIATION ; TISSUE ; COMPLEX ; COMPLEXES ; FAMILY ; primary ; DOMAIN ; TISSUES ; BIOLOGY ; MEMBER ; MEMBERS ; polymorphism ; ELEMENT ; PATTERNS ; ELEMENTS ; NUCLEUS ; CRYSTAL-STRUCTURE ; MUSCLE ; STABILITY ; tomography ; intermediate filaments ; INTERMEDIATE-FILAMENTS ; Jun ; keratin ; vimentin ; epidermis ; DIMER ; ATOMIC-STRUCTURE ; intermediate filament ; molecular ; ONCOLOGY ; PROGRAM ; review ; RE ; FAMILIES ; PATTERN ; ELECTRON-MICROSCOPY ; assembly ; COILED-COIL ; EPIDERMAL KERATIN FILAMENTS ; ROD DOMAIN ; analysis ; methods ; LONG ; USA ; FILAMENTS ; STEM ; modeling ; X-RAY ; SHAPE ; cryo-electron tomography ; FIBROUS PROTEINS ; HELICAL COILED COILS ; IV ALPHA-INTERNEXIN ; PLASTICITY ; small-angle X-ray scattering ; TRICHOCYTE KERATIN
    Abstract: Intermediate filaments (IFs) represent one of the prominent cytoskeletal elements of metazoan cells. Their constituent proteins are coded by a multigene family, whose members are expressed in complex patterns that are controlled by developmental programs of differentiation. Hence, IF proteins found in epidermis differ significantly from those in muscle or neuronal tissues. Due to their fibrous nature, which stems from a fairly conserved central alpha-helical coiled-coil rod domain, IF proteins have long resisted crystallization and thus determination of their atomic structure. Since they represent the primary structural elements that determine the shape of the nucleus and the cell more generally, a major challenge is to arrive at a more rational understanding of how their nanomechanical properties effect the stability and plasticity of cells and tissues. Here, we review recent structural results of the coiled-coil dimer, assembly intermediates and growing filaments that have been obtained by a hybrid methods approach involving a rigorous combination of X-ray crystallography, small angle X-ray scattering, cryo-electron tomography, computational analysis and molecular modeling. (c) 2007 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 17521629
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  • 5
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    BMC Biology 9 (), Art.Nr.16- 
    Keywords: CELLS ; PROTEIN ; lamin ; ARCHITECTURE ; NUCLEAR
    Abstract: Intermediate filaments include the nuclear lamins, which are universal in metazoans, and the cytoplasmic intermediate filaments, which are much more varied and form cell type-specific networks in animal cells. Until now, it has been thought that insects harbor lamins only. This view is fundamentally challenged by the discovery, reported in BMC Biology, of an intermediate filament-like cytoplasmic protein, isomin, in the hexapod Isotomurus maculatus. Here we briefly review the history of research on intermediate filaments, and discuss the implications of this latest finding in the context of what is known of their structure and functions
    Type of Publication: Journal article published
    PubMed ID: 21356127
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  • 6
    Keywords: IN-VITRO ; CELL ; Germany ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; DOMAIN ; BIOLOGY ; ASSOCIATION ; polymer ; CAENORHABDITIS-ELEGANS ; intermediate filaments ; vimentin ; BUILDING-BLOCKS ; ATOMIC-STRUCTURE ; assembly ; SCIENCE ; coiled coil ; analytical ultracentrifugation ; KERATIN INTERMEDIATE-FILAMENTS ; FRAGMENT ; CELL ARCHITECTURE ; EXPRESSION PATTERN ; NUCLEAR LAMIN ; STRUCTURAL ELEMENTS ; glycerol spraying ; rotary metal ; shadowing electron microscopy
    Abstract: Half-minilamins, representing amino- and carboxy-terminal fragments of human lamins A, B1 and B2 with a truncated central rod domain, were investigated for their ability to form distinct head-to-tail-type dimer complexes. This mode of interaction represents an essential step in the longitudinal assembly reaction exhibited by full-length lamin dimers. As determined by analytical ultracentrifugation, the amino-terminal fragments were soluble under low ionic strength conditions sedimenting with distinct profiles and s-values (1.6-1.8 S) indicating the formation of coiled-coil dimers. The smaller carboxy-terminal fragments were, except for lamin B2, largely insoluble under these conditions. However, after equimolar amounts of homotypic amino- and carboxy-terminal lamin fragments had been mixed in 4 M urea, upon subsequent renaturation the carboxyterminal fragments were completely rescued from precipitation and distinct soluble complexes with higher s-values (2.3-2.7 S) were obtained. From this behavior, we conclude that the amino- and carboxy-terminal coiled-coil dimers interact to form distinct oligomers (i.e. tetramers). Furthermore, a corresponding interaction occurred also between heterotypic pairs of A- and B-type lamin fragments. Hence, A-type lamin dimers may interact with B-type lamin dimers head-to-tail to yield linear polymers. These findings indicate that a lamin dimer principally has the freedom for a "combinatorial" head-to-tail association with all types of lamins, a property that might be of significant importance for the assembly of the nuclear lamina. Furthermore, we suggest that the head-to-tail interaction of the rod end domains represents a principal step in the assembly of cytoplasmic intermediate filament proteins too. (C) 2009 Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 20004208
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  • 7
    Keywords: CELLS ; CELL ; MODEL ; MECHANISM ; DOMAIN ; BIOLOGY ; SEQUENCE ; crystal structure ; CRYSTAL-STRUCTURE ; LENGTH ; intermediate filaments ; INTERMEDIATE-FILAMENTS ; vimentin ; SEGMENTS ; PROGRAM ; PATTERN ; SCIENCE ; coiled coil ; MOLECULAR ARCHITECTURE ; FRAGMENT ; CELL BIOLOGY ; Type ; CELL ARCHITECTURE ; ELECTRON-PARAMAGNETIC-RESONANCE ; Hendecad repeat ; PROTEIN CRYSTALLOGRAPHY
    Abstract: Intermediate filaments (IFS) are essential cytoskeletal components in metazoan cells. They assemble from elementary dimers that are built around the central alpha-helical coiled-coil rod domain representing the IF 'signature'. The rod consists of two similarly-sized parts, coil 1 and coil 2, connected by a non-alpha-helical linker L12. Coil 2 is absolutely conserved in length across all IF types and was initially predicted to consist of a short coiled-coil segment 2A based on a heptad pattern of hydrophobic residues, another linker L2 and a coiled-coil segment 2B. Here we present the crystal structure of human vimentin fragment including residues 261-335 i.e. approximately the first half of coil 2. The N-terminal part of this fragment reveals a parallel alpha-helical bundle characterized by 3.5 consecutive hendecad repeats. It is immediately followed by a regular left-handed coiled coil. The distinct non-helical linker L2 is therefore not observed. Together with the previously determined crystal structure of the major part of segment 2B (Strelkov et al., 2002), we can now build a complete atomic model of the 21 nm long vimentin coil 2 dimer being a relatively rigid rod. (C) 2010 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 20176112
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  • 8
  • 9
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    BioEssays 25 (3), 243-251 
    Keywords: CELLS ; MODEL ; MODELS ; NETWORK ; PROTEIN ; PROTEINS ; COMPLEX ; DYNAMICS ; SEQUENCE ; ASSOCIATION ; CRYSTAL-STRUCTURE ; MICROTUBULES ; intermediate filaments ; keratin ; vimentin ; FRAGMENTS ; DIMER ; ARCHITECTURE ; ATOMIC-STRUCTURE ; tetramer ; COILED COILS
    Abstract: Together with microtubules and actin microfilaments, similar to11 nm wide intermediate filaments (IFs) constitute the integrated, dynamic filament network present in the cytoplasm of metazoan cells. This network is critically involved in division, motility and other cellular processes. While the structures of microtubules and microfilaments are known in atomic detail, IF architecture is presently much less understood. The elementary 'building block' of IFs is a highly elongated, rod-like dimer based on an alpha-helical coiled-coil structure. Assembly of cytoplasmic IF proteins, such as vimentin, begins with a lateral association of dimers into tetramers and gradually into the so-called unit-length filaments (ULFs). Subsequently ULFs start to anneal longitudinally, ultimately yielding mature IFs after a compaction step. For nuclear lamins, however, assembly starts with a head-to-tail association of dimers. Recently, X-ray crystallographic data were obtained for several fragments of the vimentin dimer. Based on the dimer structure, molecular models of the tetramer and the entire filament are now a possibility
    Type of Publication: Journal article published
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  • 10
    Keywords: CELLS ; CELL ; Germany ; human ; SYSTEM ; SYSTEMS ; DISEASE ; DISEASES ; DISTINCT ; PROTEIN ; PROTEINS ; BIOLOGY ; ELEMENT ; STRESS ; MUTATION ; LINE ; PATHOGENESIS ; MUTATIONS ; NUCLEUS ; MUSCLE ; cytoskeleton ; intermediate filaments ; INTERMEDIATE-FILAMENTS ; ATOMIC-FORCE MICROSCOPY ; MUSCULAR-DYSTROPHY ; MICE LACKING VIMENTIN ; ARCHITECTURE ; intermediate filament ; DYSTROPHY ; muscular dystrophy ; review ; RE ; NUCLEAR LAMINA ; analysis ; function ; animal ; FILAMENTS ; physiological function ; CYTOPLASM ; DESMIN CYTOSKELETON ; FOCAL ADHESIONS ; MECHANOTRANSDUCTION
    Abstract: Intermediate filaments (IFs) constitute a major structural element of animal cells. They build two distinct systems, one in the nucleus and one in the cytoplasm. In both cases, their major function is assumed to be that of a mechanical stress absorber and an integrating device for the entire cytoskeleton. In line with this, recent disease mutations in human IF proteins indicate that the nanomechanical properties of cell-type-specific IFs are central to the pathogenesis of diseases as diverse as muscular dystrophy and premature ageing. However, the analysis of these various diseases suggests that IFs also have an important role in cell-type-specific physiological functions
    Type of Publication: Journal article published
    PubMed ID: 17551517
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