Human periostin is a 78–91 kDa matricellular protein
implicated
in extracellular matrix remodeling, tumor development, metastasis,
and inflammatory diseases like atopic dermatitis, psoriasis, and asthma.
The protein consists of six domains, including an N-terminal Cys-rich
CROPT domain, four fasciclin-1 domains, and a C-terminal domain. The
exons encoding the C-terminal domain may be alternatively spliced
by shuffling four exons, generating ten variants of unknown function.
Here, we investigate the structure and interactome of the full-length
variant of the C-terminal domain with no exons spliced out. The structural
analysis showed that the C-terminal domain lacked a tertiary structure
and was intrinsically disordered. In addition, we show that the motif
responsible for heparin-binding is in the conserved very C-terminal
part of periostin. Pull-down confirmed three known interaction partners
and identified an additional 140 proteins, among which nine previously
have been implicated in atopic dermatitis. Based on our findings,
we suggest that the C-terminal domain of periostin facilitates interactions
between connective tissue components in concert with the four fasciclin
domains.