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Published online December 31, 2007
doi:10.1083/jcb.200707045
The Journal of Cell Biology, Vol. 179, No. 7, 1583-1597
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Jani et al.
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Article

 Zasp is required for the assembly of functional integrin adhesion sites

Klodiana Jani and Frieder Schöck

Department of Biology, McGill University, Montreal, Quebec H3A 1B1, Canada

Correspondence to Frieder Schöck: frieder.schoeck{at}mcgill.ca

The integrin family of heterodimeric transmembrane receptors mediates cell–matrix adhesion. Integrins often localize in highly organized structures, such as focal adhesions in tissue culture and myotendinous junctions in muscles. Our RNA interference screen for genes that prevent integrin-dependent cell spreading identifies Z band alternatively spliced PDZ-motif protein (zasp), encoding the only known Drosophila melanogaster Alp/Enigma PDZ-LIM domain protein. Zasp localizes to integrin adhesion sites and its depletion disrupts integrin adhesion sites. In tissues, Zasp colocalizes with βPS integrin in myotendinous junctions and with {alpha}-actinin in muscle Z lines. Zasp also physically interacts with {alpha}-actinin. Fly larvae lacking Zasp do not form Z lines and fail to recruit {alpha}-actinin to the Z line. At the myotendinous junction, muscles detach in zasp mutants with the onset of contractility. Finally, Zasp interacts genetically with integrins, showing that it regulates integrin function. Our observations point to an important function for Zasp in the assembly of integrin adhesion sites both in cell culture and in tissues.

Abbreviations used in this paper: dsRNA, double-stranded RNA; Zasp, Z band alternatively spliced PDZ-motif protein.


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