C-terminally truncated kindlin-1 leads to abnormal adhesion and migration of keratinocytes

C. Has, R. J. Ludwig, C. Herz, J. S. Kern, S. Ussar, F. R. Ochsendorf, R. Kaufmann, H. Schumann, J. Kohlhase, L. Bruckner-Tuderman*

*Corresponding author for this work
15 Citations (Scopus)


Background: The Kindler syndrome (KS) protein kindlin-1 is a member of a protein complex that links cortical actin to integrins on the surface of basal keratinocytes. Loss of kindlin-1 leads to abnormalities of cell adhesion and motility, and to skin blistering and progressive poikiloderma as clinical symptoms. Objectives: Here we investigated a severely affected patient, disclosed the mutation that caused the disease and delineated its biological consequences. Methods: Mutation screening of the kindlin-1 gene, KIND1 (now called FERMT1), was performed with polymerase chain reaction (PCR) amplification of all exons and sequencing. Mutated kindlin-1 was characterized by reverse transcriptase (RT)-PCR and immunoblotting, and genotype-phenotype correlations were analysed using immunohistochemical staining of skin biopsies and keratinocytes from the patient's skin. Cell adhesion and motility were assessed with functional tests. Results: We disclosed a splice site mutation in the first position of intron 13 of the FERMT1 gene, which caused skipping of exon 13. The short transcript partially escaped nonsense-mediated mRNA decay and was translated into a truncated protein. Conclusion: A C-terminally truncated kindlin-1 in keratinocytes could not function correctly even if it were expressed.

Original languageEnglish
JournalBritish Journal of Dermatology
Issue number5
Pages (from-to)1192-1196
Number of pages5
Publication statusPublished - 01.11.2008


Dive into the research topics of 'C-terminally truncated kindlin-1 leads to abnormal adhesion and migration of keratinocytes'. Together they form a unique fingerprint.

Cite this