JCI table of contents, November 15 2004

dney disease

Approximately 1 in 1,000 individuals are affected by polycystic kidney disease, characterized by the development of multiple cysts in the kidney and end-stage renal disease in late middle age. Resulting from mutations in 1 of 2 genes, PKD1 or PKD2, previous studied have presupposed that the proteins encoded by these two genes, polycystin-1 and 2, physically interact to initiate a number of cell signaling cascades. However, recent studies have shown that these two proteins are located in different compartments with the cell, begging the question how can they interact?

In the November 15 issue of the Journal of Clinical Investigation, Michael Caplan and colleagues provide the first evidence that the tail of the cell surface receptor polycystin-1 is cleaved and released from the cell membrane by a process known as regulated intramembrane proteolysis where it then travels to the nucleus in a polycystin-2dependent manner to modulate gene expression. This explains how polycystin-1polycystin-2 interactions occur without colocalization of these proteins in the same membrane compartment.

In an accompanying commentary, Lisa Guay-Woodford from the University of Alabama at Birmingham discusses how this highly choreographed cellular crosstalk may affect other signaling pathways within the cell that ultimately define and maintain normal kidney cell architecture.

TITLE: Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus.

AUTHOR CONTACT: Michael J. Caplan
Department of Cellular and Molecular Physiology, Yale University, New Haven, Connecticut, USA.
Phone: 203-785-7316; Fax: 203-785-4951; E-mail: michael.caplan@yale.edu.

View the PDF of this article at: https://www.the-jci.org

Contact: Brooke Grindlinger
Journal of Clinical Investigation

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