ArticleMolecular biology of the cell2005
Defining the properties of the nonhelical tail domain in type II keratin 5: insight from a bullous disease-causing mutation.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.Structure (London, England : 1993) · 2020Article
- Epithelial cell migration requires the interaction between the vimentin and keratin intermediate filaments.Scientific reports · 2016Article
- Functional Analysis of Keratin-Associated Proteins in Intestinal Epithelia: Heat-Shock Protein Chaperoning and Kinase Rescue.Methods in enzymology · 2016Article
- Identification of novel interaction between annexin A2 and keratin 17: evidence for reciprocal regulation.The Journal of biological chemistry · 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
- Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility.The Journal of clinical investigation · 2009Review
- Hedgehog signaling, keratin 6 induction, and sebaceous gland morphogenesis: implications for pachyonychia congenita and related conditions.The American journal of pathology · 2008Article
- The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27.American journal of human genetics · 2006Article
- Multiple roles for keratin intermediate filaments in the regulation of epithelial barrier function and apico-basal polarity.Tissue barriersReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Inherited mutations in the intermediate filament (IF) proteins keratin 5 (K5) or keratin 14 (K14) cause epidermolysis bullosa simplex (EBS), in which basal layer keratinocytes rupture upon trauma to the epidermis. Most mutations are missense alleles affecting amino acids located in the central alpha-helical rod domain of K5 and K14. Here, we study the properties of an unusual EBS-causing mutation in which a nucleotide deletion (1649delG) alters the last 41 amino acids and adds 35 residues to the C terminus of K5. Relative to wild type, filaments coassembled in vitro from purified K5-1649delG and K14 proteins are shorter and exhibit weak viscoelastic properties when placed under strain. Loss of the C-terminal 41 residues contributes to these alterations. When transfected in cultured epithelial cells, K5-1649delG incorporates into preexisting keratin IFs and also forms multiple small aggregates that often colocalize with hsp70 in the cytoplasm. Aggregation is purely a function of the K5-1649delG tail domain; in contrast, the cloned 109 residue-long tail domain from wild type K5 is distributed throughout the cytoplasm and colocalizes partly with keratin IFs. These data provide a mechanistic basis for the cell fragility seen in individuals bearing the K5-1649delG allele, and point to the role of the C-terminal 41 residues in determining K5's assembly properties.
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