The isolated polycystin-1 COOH-terminal can activate or block polycystin-1 signaling

Uma Basavanna, Kimberly M. Weber, Qinghua Hu, Roy C. Ziegelstein, Gregory G. Germino, Michael Sutters

Research output: Contribution to journalArticle

Abstract

Much of what is known of the activities of polycystin-1 has been inferred from the effects of the isolated cytoplasmic COOH-terminal domain, but it is not clear whether the truncation acts like polycystin-1, as a dominant negative, or in unrelated pathways. To address this question, we have examined functional interactions between the intact and truncated forms of polycystin-1 in one cell system. In cells expressing only native polycystin-1, introduction of the truncation replicated the activity of the full-length protein. Conversely, when background levels of polycystin-1 were modestly elevated, the truncation acted as a dominant negative. Hence, the truncation acts in the polycystin pathway, but with effects that depend upon the background level of polycystin-1 expression. Our data raise the possibility that the cytoplasmic carboxyl terminus, either through cleavage products or intramolecular interactions, might feed back to modulate the activity of parent or intact polycystin-1.

Original languageEnglish (US)
Pages (from-to)367-372
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume359
Issue number2
DOIs
StatePublished - Jul 27 2007

Keywords

  • Apoptosis
  • Autosomal dominant polycystic kidney disease
  • Cell calcium
  • Endoplasmic reticulum
  • Polycystin-1
  • Proliferation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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