Type I Keratin 17 Protein Is Phosphorylated on Serine 44 by p90 Ribosomal Protein S6 Kinase 1 in a Growth- and Stress-Dependent Fashion

    Xiaoou Pan, Lesley A. Kane, Jennifer E. Van Eyk, Pierre A. Coulombe
    Studysummary This study found that serine 44 in the N-terminal head domain of keratin 17 is phosphorylated in response to various stimuli affecting skin keratinocyte growth, linking K17 up-regulation with growth and stress responses in skin epithelium.
    Automatically generated from the study's abstract, not written by a person, and not a review of the full paper. Not medical advice or a treatment recommendation. Read the original study, and consult a qualified healthcare professional before changing treatment. Full disclaimer
    Read the full study on jbc.org →
    Discuss this study in the Community →

    Research cited in this study 6

    1. Keratin 17 Modulates Hair Follicle Cycling in a TNFα-Dependent Fashion Genes & Development · 2006
    2. Keratin 17 Null Mice Exhibit Age- And Strain-Dependent Alopecia Genes & Development · 2002
    3. Type II Keratins Are Phosphorylated on a Unique Motif During Stress and Mitosis in Tissues and Cultured Cells Molecular Biology of the Cell · 2002
    4. Onset of Keratin 17 Expression Coincides with the Definition of Major Epithelial Lineages During Skin Development The Journal of Cell Biology · 1998
    5. Keratin 17 Mutations Cause Either Steatocystoma Multiplex or Pachyonychia Congenita Type 2 British Journal of Dermatology · 1998
    6. Keratin Expression in Basal Cell Carcinomas British Journal of Dermatology · 1992