The Isolated Polycystin-1 Cooh-terminal Can Activate or Block Polycystin-1 Signaling.
From: Division of Nephrology, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Biochemical and biophysical research communications
- Publish Date: Jul 2007
- ISSN: 0006-291X
- Volume: 359
- Issue: 2
- Pages: 367-72
- Medium: Print
- Language: English
- Citation (JAMA): Basavanna Uma, Weber Kimberly M, Hu Qinghua, et al. The Isolated Polycystin-1 Cooh-terminal Can Activate or Block Polycystin-1 Signaling.. Biochem. Biophys. Res. Commun. Jul 2007;359:367-72
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.
Mesh Headings (Keywords): Animals, Apoptosis, Calcium, Cell Line, Cells, Cultured, Cytoplasm, Dogs, Endoplasmic Reticulum, Genes, Dominant, Humans, Models, Biological, Polycystic Kidney Diseases, Protein Structure, Tertiary, Signal Transduction, TRPP Cation Channels
Check for Full Text / PubMed Unique Identifier (PMID): 17540339
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