Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly

Herrmann, Harald; Hofmann, Ilse; Franke, Werner W.

doi:10.1016/0022-2836(92)90980-x

Cited by 158 publications

(100 citation statements)

References 61 publications

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“…Recombinant vimentin was purified and stored in tetramer buffer (5 mM Tris-HCl, pH 7.4, 1 mM DTT) containing 8 M urea, 1 mM EDTA, 0.1 mM EGTA, and 10 mM methyl ammonium chloride (25). Prior to use, vimentin was dialyzed at 4°C for 30-min intervals in tetramer buffer containing 6, 4, and 2 M urea and then overnight in tetramer buffer.…”

Section: Sterol-binding Assays-[mentioning

confidence: 99%

Oxysterol-binding Protein (OSBP)-related Protein 4 (ORP4) Is Essential for Cell Proliferation and Survival

Charman¹,

Colbourne²,

Pietrangelo³

et al. 2014

Journal of Biological Chemistry

118

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Background:The function of oxysterol-binding protein-related protein (ORP4) is unknown. Results: Silencing ORP4L or all ORP4 isoforms triggers growth arrest and apoptosis, which is suppressed by H-Ras and involves the C-terminal lipid binding domain. Conclusion: ORP4 is a sterol and PI-4P-binding protein required for survival and proliferation of immortalized and transformed cells. Significance: This is the first study to identify a mammalian ORP with growth regulatory activity.

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Section: Sterol-binding Assays-[mentioning

confidence: 99%

Oxysterol-binding Protein (OSBP)-related Protein 4 (ORP4) Is Essential for Cell Proliferation and Survival

Charman¹,

Colbourne²,

Pietrangelo³

et al. 2014

Journal of Biological Chemistry

118

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“…6), except for the divergent hair keratins, and lie at the transition between the V1 (variable) and the H1 (hypervariable) subdomains in the non-helical head domain of the protein. Head domains of intermediate filaments are known to be essential for filament assembly (Hatzfeld and Burba, 1994;Herrmann et al, 1992) and are now being increasingly implicated in interactions between intermediate filaments and a variety of other proteins (Candi et al, 1998;Meng et al, 1997). The H1 domain, and H2 in the tail, flank the α-helical rod domain and contain phosphorylation sites essential for remodelling the filament networks.…”

Section: Possible Consequences Of Altered K8 Conformationmentioning

confidence: 99%

Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients

Owens

Wilson

Hill

et al. 2004

Journal of Cell Science

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We have identified miss-sense mutations in keratin 8 in a subset of patients with inflammatory bowel disease (Crohn disease and ulcerative colitis). Inflammatory bowel diseases are a group of disorders that are polygenic in origin and involve intestinal epithelial breakdown. We investigated the possibility that these keratin mutations might contribute to the course of the disease by adversely affecting the keratin filament network that provides mechanical support to cells in epithelia. The mutations (Gly62 to Cys, Ile63 to Val and Lys464 to Asn) all lie outside the major mutation hotspots associated with severe disease in epidermal keratins, but using a combination of in vitro and cell culture assays we show that they all have detrimental effects on K8/K18 filament assembly in vitro and in cultured cells. The G62C mutation also gives rise to homodimer formation on oxidative stress to cultured intestinal epithelial cells, and homodimers are known to be polymerization incompetent. Impaired keratin assembly resulting from the K8 mutations found in some inflammatory bowel disease patients would be predicted to affect the maintenance and re-establishment of mechanical resilience in vivo, as required during keratin cytoskeleton remodeling in cell division and differentiation, which may lead to epithelial fragility in the gut. Simple epithelial keratins may thus be considered as candidates for genes contributing to a risk of inflammatory bowel disease.

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“…Whereas the aminoterminal domain, the head domain, is indispensable for assembly of vimentin proteins into ®laments, truncation of the carboxyterminal domain, the tail domain, does not prevent this assembly process, but seems to a ect the arrangement of these ®laments into a proper network within the cell (Eckelt et al, 1992;Herrmann et al, 1992;McCormick et al, 1993;Traub and Vorgias, 1983). IF-de®cient C6D10 cells were transfected with an expression vector coding for a vimentin protein lacking the carboxyterminal tail domain due to the presence of a stop codon at the end of the rod domain coding sequence.…”

Section: Cells Expressing a Tail-less Vimentin Protein Accumulate Tspmentioning

confidence: 99%

Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (Vimentin) scaffold

Klotzsche

Hohenberg

et al. 1998

Oncogene

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The temperature-sensitive mutant tsp53 val135 accumulates in the cytoplasm of cells kept at the non-permissive temperature (398C), but is rapidly transported into the cell nucleus at the permissive temperature (308C). tsp53 thus may serve as a model for analysing cellular parameters in¯uencing the subcellular location of p53. Here we provide evidence that retention of tsp53 in the cytoplasm at the non-permissive temperature is due to cytoskeletal anchorage of the p53 protein. Two sublines of C6 rat glioma cells di ering in their expression of the intermediate ®lament protein vimentin (vimentin expressing or vimentin negative cells) were stably transfected with a vector encoding tsp53. Whereas cells of vimentin expressing C6 subclones retained tsp53 in the cytoplasm at the non-permissive temperature, cells of vimentin negative subclones exclusively harbored the tsp53 within their nuclei. Intermediate ®lament de®cient cells that had been reconstituted with a full length vimentin protein again showed a cytoplasmic localization of tsp53, whereas in cells expressing a C-terminally truncated (tail-less) vimentin tsp53 localized to the nucleus. We conclude that cytoplasmic sequestration of tsp53 requires an intact intermediate ®lament system.

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Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly

Cited by 158 publications

References 61 publications

Oxysterol-binding Protein (OSBP)-related Protein 4 (ORP4) Is Essential for Cell Proliferation and Survival

Oxysterol-binding Protein (OSBP)-related Protein 4 (ORP4) Is Essential for Cell Proliferation and Survival

Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients

Cytoplasmic retention of mutant tsp53 is dependent on an intermediate filament protein (Vimentin) scaffold

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