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Am J Physiol Renal Physiol 288: F345-F352, 2005. First published October 19, 2004; doi:10.1152/ajprenal.00235.2004
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Differential localization of mammalian Lin-7 (MALS/Veli) PDZ proteins in the kidney

Olav Olsen,1,2 James B. Wade,1 Nick Morin,1 David S. Bredt,2 and Paul A. Welling1,2

2Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland; and 1Department of Physiology, University of California, San Francisco, California

Submitted 25 June 2004 ; accepted in final form 6 October 2004

Lin-7 PDZ proteins, also called MALS or Velis, have been shown to coordinate basolateral membrane expression of various target proteins in renal epithelial cell models. Three different Lin-7/MALS/Veli isoforms, encoded by separate genes, have been identified. Here, we show that each Lin-7/MALS/Veli isoform is expressed in the kidney. Using MALS isoform-specific antibodies in combination with cell-specific marker antibodies, we found the products of the three mammalian Lin-7/MALS/Veli genes are differentially expressed along the length of the nephron. MALS/Veli 1 is predominately expressed in the glomerulus, thick ascending limb of Henle’s loop (TAL), and the distal convoluted tubule (DCT). MALS/Veli 2 is exclusively expressed in the vasa recta. MALS/Veli 3 is largely located in the DCT and collecting duct. The subcellular localization of MALS/Veli proteins can vary, depending on the isoform and the cell type. In contrast to the predominate basolateral location of MALS/Veli 1 in the TAL and DCT and MALS/Veli 3 in the DCT, MALS/Veli 1 is found diffusely throughout the cytosol of intercalated cells. In the collecting duct, MALS/Veli 3 is chiefly located on the basal membrane. Collectively, these results suggest that different MALS/Veli isoforms may carry out cell type-specific functions. The TAL and distal segments appear to have the most significant capacity for a basolateral membrane-targeting mechanism involving different MALS/Veli isoforms.

polarity; epithelial; basolateral membrane; apical membrane; CASK; synapse-associated protein-97


Address for reprint requests and other correspondence: P. A. Welling, Dept. of Physiology, Univ. of Maryland School of Medicine, 655 W. Baltimore St., Balimore, MD 21201 (E-mail: pwelling{at}umaryland.edu)




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