scholarly journals Affinity to cellulose is a shared property among coiled-coil domains of intermediate filaments and prokaryotic intermediate filament-like proteins

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Niklas Söderholm ◽  
Ala Javadi ◽  
Isabel Sierra Flores ◽  
Klas Flärdh ◽  
Linda Sandblad
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
Shared Property

Plectin: A Cytolinker by Design

1999 ◽  
Vol 380 (2) ◽  
pp. 151-158 ◽  
Author(s):  
F.A. Steinböck ◽  
G. Wiche
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Transmembrane Protein ◽  
Coiled Coil ◽  
Cytoskeletal Protein ◽  
Terminal Domain ◽  
Junctional Proteins ◽  
Molecular Backbone ◽  
Cytoskeletal Elements

Abstract Plectin is a cytoskeletal protein of > 500 kDa that forms dumbbell-shaped homodimers comprising a central parallel α-helical coiled coil rod domain flanked by globular domains, thus providing a molecular backbone ideally suited to mediate the protein's interactions with an array of other cytoskeletal elements. Plectin self-associates and interacts with actin and intermediate filament cytoskeleton networks at opposite ends, and it binds at both ends to the hemidesmosomal transmembrane protein integrin beta-4, and likely to other junctional proteins. The central coiled coil rod domain can form bridges over long stretches and serves as a flexible linker between the structurally diverse N-terminal domain and the highly conserved C-terminal domain. Plectin is also a target of p34cdc2 kinase that regulates its dissociation from intermediate filaments during mitosis.

Intermediate filaments: molecular architecture, assembly, dynamics and polymorphism

1999 ◽  
Vol 32 (2) ◽  
pp. 99-187 ◽  
Author(s):  
David A. D. Parry ◽  
Peter M. Steinert
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Tertiary Structure ◽  
Quaternary Structure ◽  
Lattice Structure ◽  
Coiled Coil ◽  
Salt Bridges ◽  
Molecular Architecture

1. Introduction 1002. Molecular architecture 1072.1 Primary structure 1082.1.1 Homologous regions 1092.1.2 Chain typing 1152.1.3 Post-translational modifications 1172.2 Secondary structure 1182.2.1 Central rod domain 1182.2.2 Head and tail domains 1192.3 Tertiary structure 1232.3.1 Coiled-coil rod domain 1232.3.1.1 Specificity through salt bridges 1242.3.1.2 Specificity through apolar interactions 1272.3.1.3 A consensus trigger sequence for two-stranded coiled-coils 1282.3.2 Discontinuities in the rod domain 1282.3.2.1 Links 1292.3.2.2 Stutter 1312.3.3 Head and tail domains 1312.4 Electron microscope observations 1333. Assembly 1363.1 Role of the coiled-coil rod domain 1373.2 Role of end domains 1413.3 Experimentally induced crosslinks and modes of assembly 1453.4 Naturally occurring crosslinks for tissue coordination 1543.5 STEM data 1544. Quaternary structure 1604.1 Protofilaments and protofibrils 1604.2 Head and tail domains 1634.3 Surface lattice structure 1644.4 Crystal studies on intermediate filament fragments 1685. Polymorphism 1695.1 Variations on a theme 1705.1.1 Axial structure 1705.1.2 Lateral structure 1716. Keratin intermediate filament chains in diseases 1727. Concluding remarks 1758. Acknowledgments 1769. References 176Three types of intracellular filament have been identified in eukaryotic cells, and together they constitute the key elements of the cytoskeleton. They are the microtubules, the actin-containing microfilaments and the intermediate filaments. The uniqueness of the former two types of filament in cells has been well known for a long time but, in contrast, the intermediate filaments have been a relative new-comer to the scene. The microtubules and the microfilaments have always been easy to distinguish from one another on the grounds of their respective sizes (microtubules are about 25 nm in diameter and microfilaments are about 7–10 nm in diameter). Additionally, microtubules were capable of being disaggregated by the action of colchicine, and microfilaments could be disassembled by other drugs or be decorated with heavy meromyosin to generate arrowhead-like structures. Importantly, in both microtubules and microfilaments the constituent protein subunits were arranged to give the filaments a directionality, and the ability of these filaments to function in vivo depended crucially on this feature of their structure. Microtubules, for example, are involved in mitosis, motility and transport within the cell: each of these functions is clearly a ‘directional’ one. With this background the discovery and characterization of the intermediate filaments can begin.

scholarly journals Dynamic structural order of a low complexity domain facilitates assembly of intermediate filaments

2020 ◽  
Author(s):  
Vasily O. Sysoev ◽  
Masato Kato ◽  
Lillian Sutherland ◽  
Rong Hu ◽  
Steven L. McKnight ◽  
...  
Keyword(s):  
Protein Folding ◽  
Intermediate Filaments ◽  
Cell Morphology ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
Low Complexity ◽  
Tail Domain ◽  
Sequence Complexity ◽  
New Form

AbstractThe coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiled-coil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent upon either “head” or “tail” domains of low sequence complexity. Here we confirm that the tail domain required for assembly of Drosophila Tm1 IFs functions by forming labile cross-β interactions. These interactions are seen in polymers made from the tail domain alone as well as assembled IFs formed by the intact Tm1 protein. The ability to visualize such interactions in situ within the context of a discrete cellular assembly lends support to the concept that equivalent interactions may be used in organizing other dynamic aspects of cell morphology.One Sentence SummaryA new form of protein folding that interconverts between the structured and unstructured states controls assembly of intermediate filaments.

scholarly journals Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments

2020 ◽  
Vol 117 (38) ◽  
pp. 23510-23518
Author(s):  
Vasiliy O. Sysoev ◽  
Masato Kato ◽  
Lillian Sutherland ◽  
Rong Hu ◽  
Steven L. McKnight ◽  
...  
Keyword(s):  
Intermediate Filaments ◽  
Cell Morphology ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
Low Complexity ◽  
Tail Domain ◽  
C Protein ◽  
Sequence Complexity ◽  
Structural Order

The coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiled-coil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent on either “head” or “tail” domains of low sequence complexity. Here we confirm that the tail domain required for assembly ofDrosophilaTm1-I/C IFs functions by forming labile cross-β interactions. These interactions are seen in polymers made from the tail domain alone, as well as in assembled IFs formed by the intact Tm1-I/C protein. The ability to visualize such interactions in situ within the context of a discrete cellular assembly lends support to the concept that equivalent interactions may be used in organizing other dynamic aspects of cell morphology.

scholarly journals Effects of mechanical tension on protrusive activity and microfilament and intermediate filament organization in an epidermal epithelium moving in culture.

1986 ◽  
Vol 102 (4) ◽  
pp. 1400-1411 ◽  
Author(s):  
J Kolega
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Mechanical Tension ◽  
Cytoskeletal Organization ◽  
Structural Support ◽  
Transmission Electron ◽  
Locomotive Activity ◽  
Filament Surface

Mechanical tension influences tissue morphogenesis and the synthetic, mitotic, and motile behavior of cells. To determine the effects of tension on epithelial motility and cytoskeletal organization, small, motile clusters of epidermal cells were artificially extended with a micromanipulated needle. Protrusive activity perpendicular to the axis of tension was dramatically suppressed. To determine the ultrastructural basis for this phenomenon, cells whose exact locomotive behavior was recorded cinemicrographically were examined by transmission electron microscopy. In untensed, forward-moving lamellar protrusions, microfilaments appear disorganized and anisotropically oriented. But in cytoplasm held under tension by micromanipulation or by the locomotive activity of other cells within the epithelium, microfilaments are aligned parallel to the tension. In non-spreading regions of the epithelial margin, microfilaments lie in tight bundles parallel to apparent lines of tension. Thus, it appears that tension causes alignment of microfilaments. In contrast, intermediate filaments are excluded from motile protrusions, being confined to the thicker, more central part of the cell. They roughly follow the contours of the cell, but are not aligned relative to tension even when microfilaments in the same cell are. This suggests that the organization of intermediate filaments is relatively resistant to physical distortion and the intermediate filaments may act as passive structural support within the cell. The alignment of microfilaments under tension suggests a mechanism by which tension suppresses protrusive activity: microfilaments aligned by forces exerted through filament-surface or filament-filament interconnections cannot reorient against such force and so cannot easily extend protrusions in directions not parallel to tension.

Novel features of intermediate filament dynamics revealed by green fluorescent protein chimeras

1998 ◽  
Vol 111 (13) ◽  
pp. 1767-1778 ◽  
Author(s):  
C.L. Ho ◽  
J.L. Martys ◽  
A. Mikhailov ◽  
G.G. Gundersen ◽  
R.K. Liem
Keyword(s):  
Green Fluorescent Protein ◽  
Dynamic Behavior ◽  
Cell Lines ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Fluorescent Protein ◽  
Nih3t3 Cells ◽  
Green Fluorescent ◽  
Filament Network ◽  
Perinuclear Area

In order to study the dynamic behavior of intermediate filament networks in living cells, we have prepared constructs fusing green fluorescent protein to intermediate filament proteins. Vimentin fused to green fluorescent protein labeled the endogenous intermediate filament network. We generated stable SW13 and NIH3T3 cell lines that express an enhanced green fluorescent protein fused to the N-terminus of full-length vimentin. We were able to observe the dynamic behavior of the intermediate filament network in these cells for periods as long as 4 hours (images acquired every 2 minutes). In both cell lines, the vimentin network constantly moves in a wavy manner. In the NIH3T3 cells, we observed extension of individual vimentin filaments at the edge of the cell. This movement is dependent on microtubules, since the addition of nocodazole stopped the extension of the intermediate filaments. Injection of anti-IFA causes the redistribution or ‘collapse’ of intermediate filaments. We injected anti-IFA antibodies into NIH3T3 cells stably expressing green fluorescent protein fused to vimentin and found that individual intermediate filaments move slowly towards the perinuclear area without obvious disassembly. These results demonstrate that individual intermediate filaments are translocated during the collapse, rather than undergoing disassembly-induced redistribution. Injections of tubulin antibodies disrupt the interactions between intermediate filaments and stable microtubules and cause the collapse of the vimentin network showing that these interactions play an important role in keeping the intermediate filament network extended. The nocodazole inhibition of intermediate filament extension and the anti-IFA microinjection experiments are consistent with a model in which intermediate filaments exhibit an extended distribution when tethered to microtubules, but are translocated to the perinuclear area when these connections are severed.

scholarly journals Glial Fibrillary Acidic Protein (GFAP) in Oligodendrogliomas: A Reflection of Transient GFAP Expression by Immature Oligodendroglia

1986 ◽  
Vol 13 (4) ◽  
pp. 307-311 ◽  
Author(s):  
V. Jagadha ◽  
W.C. Halliday ◽  
L.E. Becker
Keyword(s):  
White Matter ◽  
Glial Fibrillary Acidic Protein ◽  
Tumor Cells ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Immunohistochemical Staining ◽  
Neuron Specific Enolase ◽  
Acidic Protein ◽  
Gfap Expression ◽  
S 100

ABSTRACT:Fourteen pure oligodendrogliomas were studied by light- and electronmicroscopy and immunohistochemistry to examine glial fibrillary acidic protein (GFAP) positivity in the tumors. To compare the immunohistochemical staining patterns of neoplastic oligodendroglia and immature oligodendroglia, myelination glia in the white matter of eight normal brains from children under 6 months of age were studied. The tumors possessed light microscopic and ultrastructural features characteristic of oligodendrogliomas. Microtubules were found in the cytoplasm of nine tumors on electronmicroscopy. In one, intermediate filaments and microtubules were observed in occasional tumor cells with polygonal crystalline structures in the cytoplasm. Using the peroxidase-antiperoxidase technique, all specimens were stained for GFAP, vimentin, S-100 and neuron-specific enolase (NSE). In nine tumors, variable numbers of cells with an oligodendroglial morphology reacted positively for GFAP. All tumors were positive for S-100 and negative for vimentin and NSE. The myelination glia in the eight normal brains stained positively for GFAP but not for vimentin. Vimentin is expressed by developing, reactive and neoplastic astrocytes. Thus, GFAP positivity combined with vimentin negativity in both neoplastic and immature oligodendroglia suggests that GFAP positivity in oligodendrogliomas may reflect the transient expression of this intermediate filament by immature oligodendroglia.

Interactions between peripherin and neurofilaments in cultured cells: disruption of peripherin assembly by the NF-M and NF-H subunits

1999 ◽  
Vol 77 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Jean-Martin Beaulieu ◽  
Janice Robertson ◽  
Jean-Pierre Julien
Keyword(s):  
Nervous System ◽  
Peripheral Nervous System ◽  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Cultured Cells ◽  
Intermediate Filament Protein ◽  
Physiological Conditions ◽  
Filament Protein ◽  
Filament Network ◽  
Filament Type

Neurofilaments are the principal intermediate filament type expressed by neurons. They are formed by the co-assembly of three subunits: NF-L, NF-M, and NF-H. Peripherin is another intermediate filament protein expressed mostly in neurons of the peripheral nervous system. In contrast to neurofilaments, peripherin can self-assemble to establish an intermediate filament network in cultured cells. The co-expression of neurofilaments and peripherin is found mainly during development and regeneration. We used SW13 cells devoid of endogenous cytoplasmic intermediate filaments to assess the exact assembly characteristics of peripherin with each neurofilament subunit. Our results demonstrate that peripherin can assemble with NF-L. In contrast, the co-expression of peripherin with the large neurofilament subunits interferes with peripherin assembly. These results confirm the existence of interactions between peripherin and neurofilaments in physiological conditions. Moreover, they suggest that perturbations in the stoichiometry of neurofilaments can have an impact on peripherin assembly in vivo.Key words: peripherin, neurofilament, SW13 cells, intermediate filament.

scholarly journals Interaction of Theiler’s Virus with Intermediate Filaments of Infected Cells

1998 ◽  
Vol 72 (12) ◽  
pp. 9553-9560 ◽  
Author(s):  
Patrick Nédellec ◽  
Patrick Vicart ◽  
Christine Laurent-Winter ◽  
Cécile Martinat ◽  
Marie-Christine Prévost ◽  
...  
Keyword(s):  
Intermediate Filaments ◽  
Intermediate Filament ◽  
Close Contact ◽  
Theiler's Virus ◽  
Virus Particles ◽  
Host Cell Proteins ◽  
Encephalomyelitis Virus ◽  
Infected Cells ◽  
Main Components ◽  
Filament Network

ABSTRACT Theiler’s murine encephalomyelitis virus is a neurotropic murine picornavirus which replicates permissively and causes a cytopathic effect in the BHK-21 cell line. We examined the interactions between the GDVII and DA strains of Theiler’s virus and BHK-21 host cell proteins in a virus overlay assay. We observed binding of the virions to two proteins of approximately 60 kDa. These proteins were microsequenced and identified as desmin and vimentin, two main components of the intermediate filament network. The association between desmin or vimentin and virions was demonstrated by immunoprecipitation. Anti-desmin and anti-vimentin monoclonal antibodies precipitated GDVII or DA virions from extracts of infected BHK-21 cells. The intracellular distributions of virions and of the desmin and vimentin intermediate filaments of BHK-21 cells were investigated by two-color immunofluorescence confocal microscopy. Following infection, the intermediate filament network was rearranged into a shell-like structure which surrounded a viral inclusion. Finally, close contact between GDVII virus particles and 10-nm intermediate filaments was observed by electron microscopy.

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