Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly.

@article{Schaeffer2009AnalysisOU,
  title={Analysis of uromodulin polymerization provides new insights into the mechanisms regulating ZP domain-mediated protein assembly.},
  author={C{\'e}line Schaeffer and Sara Santambrogio and Simone Perucca and Giorgio Casari and Luca Rampoldi},
  journal={Molecular biology of the cell},
  year={2009},
  volume={20 2},
  pages={
          589-99
        }
}
Uromodulin is the most abundant protein secreted in urine, in which it is found as a high-molecular-weight polymer. Polymerization occurs via its zona pellucida (ZP) domain, a conserved module shared by many extracellular eukaryotic proteins that are able to assemble into matrices. In this work, we identified two motifs in uromodulin, mapping in the linker region of the ZP domain and in between protein cleavage and glycosylphosphatidylinositol (GPI)-anchoring sites, which regulate its… CONTINUE READING
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