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JCS ePress online publication date 31 May 2005
doi: 10.1242/jcs.02408

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Research Article

Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture


Kathryn D. Curtin*, Ian A. Meinertzhagen, and Robert J. Wyman
* Author for correspondence (e-mail: kcurtin{at}uark.edu)

Basigin, an IgG family glycoprotein found on the surface of human metastatic tumors, stimulates fibroblasts to secrete matrix metalloproteases that remodel the extracellular matrix. Using Drosophila melanogaster we identify intracellular, matrix metalloprotease-independent, roles for basigin. Specifically, we found that basigin, interacting with integrin, is required for normal cell architecture in some cell types. Basigin promotes cytoskeletal rearrangements and the formation of lamellipodia in cultured insect cells. Loss of basigin from photoreceptors leads to misplaced nuclei, rough ER and mitochondria, as well as to swollen axon terminals. These changes in intracellular structure suggest cytoskeletal disruptions. These defects can be rescued by either fly or mouse basigin. Basigin and integrin colocalize to cultured cells and to the visual system. Basigin-mediated changes in the architecture of cultured cells require integrin binding activity. Basigin and integrin interact genetically to affect cell structure in the animal, possibly by forming complexes at cell contacts that help organize internal cell structure.


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