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J Biol Chem, Vol. 273, Issue 29, 18235-18241, July 17, 1998

Splice Variants of the Drosophila PS2 Integrins Differentially Interact with RGD-containing Fragments of the Extracellular Proteins Tiggrin, Ten-m, and D-Laminin 2

Michael W. Graner, Thomas A. Bunch, Stefan Baumgartner^¶, Arthur Kerschen, and Danny L. Brower^**

From the Departments of  Molecular and Cellular Biology and ^** Biochemistry, University of Arizona, Tucson, Arizona 85721, the ^¶ Friedrich Miescher-Institut, Postfach 2543, CH-4002 Basel, Switzerland, and the  Department of Cell and Molecular Biology, Lund University, Box 94, S-22100 Lund, Sweden

Two new potential ligands of the Drosophila PS2 integrins have been characterized by functional interaction in cell culture. These potential ligands are a new Drosophila laminin 2 chain encoded by the wing blister locus and Ten-m, an extracellular protein known to be involved in embryonic pattern formation. As with previously identified PS2 ligands, both contain RGD sequences, and RGD-containing fragments of these two proteins (DLAM-RGD and TENM-RGD) can support PS2 integrin-mediated cell spreading. In all cases, this spreading is inhibited specifically by short RGD-containing peptides. As previously found for the PS2 ligand tiggrin (and the tiggrin fragment TIG-RGD), TENM-RGD induces maximal spreading of cells expressing integrin containing the _PS2C splice variant. This is in contrast to DLAM-RGD, which is the first Drosophila polypeptide shown to interact preferentially with cells expressing the _{PS2 m8} splice variant. The _PS integrin subunit also varies in the presumed ligand binding region as a result of alternative splicing. For TIG-RGD and TENM-RGD, the  splice variant has little effect, but for DLAM-RGD, maximal cell spreading is supported only by the _PS4A form of the protein. Thus, the diversity in PS2 integrins due to splicing variations, in combination with diversity of matrix ligands, can greatly enhance the functional complexity of PS2-ligand interactions in the developing animal. The data also suggest that the splice variants may alter regions of the subunits that are directly involved in ligand interactions, and this is discussed with respect to models of integrin structure.

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