Title : A role for disulfide bonding in keratin intermediate filament organization and dynamics in skin keratinocytes.

Pub. Date : 2015 Apr 13

PMID : 25869667






2 Functional Relationships(s)
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1 By comparing the properties of wild-type K14 with a completely cysteine-free variant thereof, we found that K14-dependent disulfide bonding limited filament elongation during polymerization in vitro but was necessary for the genesis of a perinuclear-concentrated network of keratin filaments, normal keratin cycling, and the sessile behavior of the nucleus and whole cell in keratinocytes studied by live imaging. Cysteine keratin 14 Mus musculus
2 Many of these phenotypes were rescued when analyzing a K14 variant harboring a single Cys residue at position 367. Cysteine keratin 14 Mus musculus