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Cleavage of polycystin-1 requires the receptor for egg jelly domain and is disrupted by human autosomal-dominant polycystic kidney disease 1-associated mutations.

Polycystin-1 plays an essential role in renal tubular morphogenesis, and disruption of its function causes cystogenesis in human autosomal-dominant polycystic kidney disease (ADPKD). We demonstrated that polycystin-1 undergoes cleavage at G protein coupled receptor proteolytic site in a process that requires the receptor for egg jelly domain. Most of the N-terminal fragment remains tethered at the cell surface, although a small amount is secreted. PKD1-associated mutations in the receptor for egg jelly domain disrupt cleavage, abolish the ability of polycystin-1 to activate signal transducer and activator of transcription-1, and induce tubulogenesis in vitro. We conclude that the cleavage of polycystin-1 is likely essential for its biologic activity.

Pubmed ID: 12482949


  • Qian F
  • Boletta A
  • Bhunia AK
  • Xu H
  • Liu L
  • Ahrabi AK
  • Watnick TJ
  • Zhou F
  • Germino GG


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

December 24, 2002

Associated Grants

  • Agency: NIDDK NIH HHS, Id: P50-DK57325

Mesh Terms

  • Amino Acid Sequence
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutation
  • Polycystic Kidney, Autosomal Dominant
  • Proteins
  • Receptors, Cell Surface
  • Signal Transduction
  • TRPP Cation Channels