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* Howard Hughes Medical Institute, Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago,
Illinois 60637; and Tensin is a focal adhesion phosphoprotein
that binds to F-actin and contains a functional Src homology 2 domain. To explore the biological functions
of tensin, we cloned the mouse tensin gene, determined
its program of expression, and used gene targeting to
generate mice lacking tensin. Even though tensin is expressed in many different tissues during embryogenesis,
tensin null mice developed normally and appeared
healthy postnatally for at least several months. Over
time, Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115
/ mice became frail because of abnormalities in their kidneys, an organ that expresses high levels of
tensin. Mice with overt signs of weakness exhibited
signs of renal failure and possessed multiple large cysts
in the proximal kidney tubules, but even in tensin null
mice with normal blood analysis, cysts were prevalent.
Ultrastructurally, noncystic areas showed typical cell-
matrix junctions that readily labeled with antibodies
against other focal adhesion molecules. In abnormal regions, cell-matrix junctions were disrupted and tubule
cells lacked polarity. Taken together, our data imply
that, in the kidney, loss of tensin leads to a weakening,
rather than a severing, of focal adhesion. All other tissues appeared normal, suggesting that, in most cases, tensin's diverse functions are redundant and may be
compensated for by other focal adhesion proteins.
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