Role of the cystine-knot motif at the C-terminus of rat mucin protein Muc2 in dimer formation and secretion.

@article{Bell2001RoleOT,
  title={Role of the cystine-knot motif at the C-terminus of rat mucin protein Muc2 in dimer formation and secretion.},
  author={Sherilyn L Bell and Gongqiao Xu and Janet F. Forstner},
  journal={The Biochemical journal},
  year={2001},
  volume={357 Pt 1},
  pages={203-9}
}
DNA constructs based on the 534-amino-acid C-terminus of rat mucin protein Muc2 (RMC), were transfected into COS cells and the resultant (35)S-labelled dimers and monomers were detected by SDS/PAGE of immunoprecipitates. The cystine-knot construct, encoding the C-terminal 115 amino acids, appeared in cell lysates as a 45 kDa dimer, but was not secreted. A construct, devoid of the cystine knot, failed to form dimers. Site-specific mutagenesis within the cystine knot was performed on a conserved… CONTINUE READING

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