ArticleThe Journal of cell biology1992
The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Structure and function of the keratin 17 tail domain associated with keratin intermediate filament organization.European journal of cell biology · 2025Article
- Review
- Effects of truncations in the N- and C-terminal domains of filensin on filament formation with phakinin in cell-free conditions and cultured cells.FEBS open bio · 2023Article
- KRT5 missense variant in a Cardigan Welsh Corgi with epidermolysis bullosa simplex.Animal genetics · 2022Article
- Genotype‒Structurotype‒Phenotype Correlations in Patients with Pachyonychia Congenita.The Journal of investigative dermatology · 2021Article
- Review
- Structural heterogeneity of cellular K5/K14 filaments as revealed by cryo-electron microscopy.eLife · 2021Article
- De novo filament formation by human hair keratins K85 and K35 follows a filament development pattern distinct from cytokeratin filament networks.FEBS open bio · 2021Article
- Recent insight into intermediate filament structure.Current opinion in cell biology · 2021Review
- A KRT6A and a Novel KRT16 Gene Mutations in Chinese Patients with Pachyonychia Congenita.International journal of general medicine · 2021Article
- Leukamenin E Induces K8/18 Phosphorylation and Blocks the Assembly of Keratin Filament Networks Through ERK Activation.International journal of molecular sciences · 2020Article
- Crystal Structure of Keratin 1/10(C401A) 2B Heterodimer Demonstrates a Proclivity for the C-Terminus of Helix 2B to Form Higher Order Molecular Contacts.The Yale journal of biology and medicine · 2020Article
- Epithelial cell migration requires the interaction between the vimentin and keratin intermediate filaments.Scientific reports · 2016Article
- BILBO1 is a scaffold protein of the flagellar pocket collar in the pathogen Trypanosoma brucei.PLoS pathogens · 2015Article
- Directed expression of a chimeric type II keratin partially rescues keratin 5-null mice.The Journal of biological chemistry · 2014Article
- Structural basis for heteromeric assembly and perinuclear organization of keratin filaments.Nature structural & molecular biology · 2012Article
- Defining keratin protein function in skin epithelia: epidermolysis bullosa simplex and its aftermath.The Journal of investigative dermatology · 2012Review
- Modeling the self-organization property of keratin intermediate filaments.Biophysical journal · 2010Article
- Self-organization of keratin intermediate filaments into cross-linked networks.The Journal of cell biology · 2009Article
- Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility.The Journal of clinical investigation · 2009Review
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type I and type II keratins form obligatory heterodimers, which self-assemble into 10-nm intermediate filaments (IFs). Like all IF proteins, they have a central alpha-helical rod domain, flanked by nonhelical head and tail domains. The IF rod is more highly conserved than head and tail, and within the rod, the carboxy R/K L L E G E sequence is more highly conserved than most other regions. Mutagenesis studies have shed some light on the roles of the head, tail, and R/K L L E G E sequence in 10-nm filament structure. However, interpretations have often been complicated in part because many of these studies have focused on transfected cells, where filament structure cannot be evaluated. Of the few in vitro assembly studies thus far conducted, comparison of keratin mutants with other IF mutants have often been difficult, due to the obligatory heteropolymeric nature of keratin IFs. In this report, we describe in vitro filament assembly studies on headless, tailless, headless/tailless, and R/K L L E G E truncated mutants of keratin 5 and its partner keratin 14. Using varying conditions of ionic strength and pH, we examine effects of analogous K5 and K14 mutations on the stability of 10-nm filament structure. Using EM, we examine effects of mutations on the ability of subunits/protofibrils to (a) elongate and (b) laterally associate. Our results demonstrate that (a) tails of K5 and K14 are required for filament stabilization; (b) the head of K5, but not of K14, is required for filament elongation and lateral alignments; and (c) the R/K L L E G E domains are required for lateral alignments, but not for filament elongation.
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