Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains

Herrmann, Harald; Häner, Markus; Brettel, Monika; Müller, Shirley A.; Goldie, Kenneth N.; Fedtke, Bettina; Lustig, Ariel; Franke, Werner W.; Aebi, Ueli

doi:10.1006/jmbi.1996.0688

Cited by 328 publications

(614 citation statements)

References 46 publications

(68 reference statements)

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“…Such filaments form a polymorphic population whose mass per length also yielded minor components with 10-13 dimers per cross section (20,27). In general, intermediate filaments and particularly NFs reconstituted in vitro exhibit a polymorphic character, but typically contain between 14 and 23 dimers per cross section (3,28). Our results suggest that native intermediate filaments may be more homogeneous than reconstituted intermediate filaments.…”

Section: Discussionmentioning

confidence: 67%

Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy

Leapman

Gallant

Reese

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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Phosphorylation plays a critical role in controlling the function of cytoskeletal assemblies but no direct method yet exists to measure the phosphorylation state of proteins at the level of individual molecules and assemblies. Herein, we apply scanning transmission electron microscopy in combination with electron energy loss spectroscopy to measure the distributions of mass and phosphorus in neurofilaments (NFs) isolated from the squid giant axon. We find that native squid NFs, in contrast to typical reconstituted intermediate filaments, are a relatively homogeneous population containing only eight coiled-coil dimers per cross section. The measured stoichiometry of ϳ1:1 for light͞heavy peptides strongly suggests that squid NFs are composed of heterodimers. Furthermore, each heavy chain of the dimers carries at least 100 phosphate groups and is, therefore, near-maximally phosphorylated. These results also demonstrate that scanning transmission electron microscopy combined with electron energy loss spectroscopy at the nanometer scale is capable of characterizing the level and distribution of phosphorylation in individual mass-mapped protein assemblies.

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Section: Discussionmentioning

confidence: 67%

Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy

Leapman

Gallant

Reese

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…Within the filament cross-section, there is an average of 16 coiled-coil dimers, as determined by mass-per-length measurements. 31 However, there are never 16 subfilaments depicted in an IF. Instead electron micrographs of unraveled filaments reveal the presence of four to eight subfilaments that coil around each other.…”

Section: Discussionmentioning

confidence: 99%

Exploring the Mechanical Properties of Single Vimentin Intermediate Filaments by Atomic Force Microscopy

Guzmán

Jeney

Kreplak

et al. 2006

Journal of Molecular Biology

106

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Intermediate filaments (IFs), together with actin filaments and microtubules, compose the cytoskeleton. Among other functions, IFs impart mechanical stability to cells when exposed to mechanical stress and act as a support when the other cytoskeletal filaments cannot keep the structural integrity of the cells. Here we present a study on the bending properties of single vimentin IFs in which we used an atomic force microscopy (AFM) tip to elastically deform single filaments hanging over a porous membrane. We obtained a value for the bending modulus of non-stabilized IFs between 300 MPa and 400 MPa. Our results together with previous ones suggest that IFs present axial sliding between their constitutive building blocks and therefore have a bending modulus that depends on the filament length. Measurements of glutaraldehyde-stabilized filaments were also performed to reduce the axial sliding between subunits and therefore provide a lower limit estimate of the Young's modulus of the filaments. The results show an increment of two to three times in the bending modulus for the stabilized IFs with respect to the non-stabilized ones, suggesting that the Young's modulus of vimentin IFs should be around 900 MPa or higher.

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“…This latter observation may be partly because nestin has only a short amino-terminal head domain. In the case of vimentin homopolymer IFs, it is known that the head domain plays an important role in dimer-dimer interaction (Herrmann et al, 1996a). Therefore, the presence of heterodimers containing only one full-length head (i.e., that of vimentin) may lead to the formation of less stable though still long IFs.…”

Section: Discussionmentioning

confidence: 99%

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

Chou

Khuon

Herrmann

et al. 2003

MBoC

Self Cite

175

153

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The expression of the intermediate filament (IF) protein nestin is closely associated with rapidly proliferating progenitor cells during neurogenesis and myogenesis, but little is known about its function. In this study, we examine the effects of nestin expression on the assembly state of vimentin IFs in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IFs into nonfilamentous aggregates or particles in mitotic but not interphase cells. This nestin-mediated disassembly of IFs is dependent on the phosphorylation of vimentin by the maturation/M-phase–promoting factor at ser-55 in the amino-terminal head domain. In addition, the disassembly of vimentin IFs during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is downregulated by the nestin-specific small interfering RNA in nestin-expressing cells, vimentin IFs remain assembled throughout all stages of mitosis. Previous studies suggest that nonfilamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. On the basis of these observations, we speculate that nestin may play a role in the trafficking and distribution of IF proteins and potentially other cellular factors to daughter cells during progenitor cell division

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Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains

Cited by 328 publications

References 46 publications

Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy

Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy

Exploring the Mechanical Properties of Single Vimentin Intermediate Filaments by Atomic Force Microscopy

Nestin Promotes the Phosphorylation-dependent Disassembly of Vimentin Intermediate Filaments During Mitosis

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