ArticleThe Journal of cell biology1990
Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 135 citations in OpenAlex.
- Bridging Nature and Engineering: Protein-Derived Materials for Bio-Inspired Applications.Biomimetics (Basel, Switzerland) · 2024Review
- Discovery of keratin function and role in genetic diseases: the year that 1991 was.Molecular biology of the cell · 2016Review
- Skin Keratins.Methods in enzymology · 2016Article
- Epithelial stem cells as mucosal antigen-delivering cells: A novel AIDS vaccine approach.Vaccine · 2015Article
- The tail domain is essential but the head domain dispensable for C. elegans intermediate filament IFA-2 function.PloS one · 2015Article
- Defining keratin protein function in skin epithelia: epidermolysis bullosa simplex and its aftermath.The Journal of investigative dermatology · 2012Review
- Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility.The Journal of clinical investigation · 2009Review
- Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin.Investigative ophthalmology & visual science · 2007Article
- Reprogramming of keratin biosynthesis by sulforaphane restores skin integrity in epidermolysis bullosa simplex.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Insights into the beaded filament of the eye lens.Experimental cell research · 2007Review
- The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro.The Journal of cell biology · 2001Article
- Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization.The Journal of cell biology · 2001Article
- A novel keratin 12 mutation in a German kindred with Meesmann's corneal dystrophy.The British journal of ophthalmology · 2000Article
- Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis.The Journal of cell biology · 1997Article
- A keratin K10 gene mutation in a Japanese patient with epidermolytic hyperkeratosis.The Japanese journal of human genetics · 1997Article
- Keith R. Porter Lecture, 1996. Of mice and men: genetic disorders of the cytoskeleton.Molecular biology of the cell · 1997Review
- The genetic basis of epidermolysis bullosa simplex with mottled pigmentation.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Epidermolysis bullosa simplex: a keratin 5 mutation is a fully dominant allele in epidermal cytoskeleton function.American journal of human genetics · 1995Article
- The importance of intramolecular ion pairing in intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Differential dynamics of neurofilament-H protein and neurofilament-L protein in neurons.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To investigate the sequences important for assembly of keratins into 10-nm filaments, we used a combined approach of (a) transfection of mutant keratin cDNAs into epithelial cells in vivo, and (b) in vitro assembly of mutant and wild-type keratins. Keratin K14 mutants missing the nonhelical carboxy- and amino-terminal domains not only integrated without perturbation into endogenous keratin filament networks in vivo, but they also formed 10-nm filaments with K5 in vitro. Surprisingly, keratin mutants missing the highly conserved L L E G E sequence, common to all intermediate filament proteins and found at the carboxy end of the alpha-helical rod domain, also assembled into filaments with only a somewhat reduced efficiency. Even a carboxy K14 mutant missing approximately 10% of the rod assembled into filaments, although in this case filaments aggregated significantly. Despite the ability of these mutants to form filaments in vitro, they often perturbed keratin filament organization in vivo. In contrast, small truncations in the amino-terminal end of the rod domain more severely disrupted the filament assembly process in vitro as well as in vivo, and in particular restricted elongation. For both carboxy and amino rod deletions, the more extensive the deletion, the more severe the phenotype. Surprisingly, while elongation could be almost quantitatively blocked with large mutations, tetramer formation and higher ordered lateral interactions still occurred. Collectively, our in vitro data (a) provide a molecular basis for the dominance of our mutants in vivo, (b) offer new insights as to why different mutants may generate different phenotypes in vivo, and (c) delineate the limit sequences necessary for K14 to both incorporate properly into a preexisting keratin filament network in vivo and assemble efficiently into 10-nm keratin filaments in vitro.
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