Reference Report

Reference
Citation	Curtin, K.D., Meinertzhagen, I.A., Wyman, R.J. (2005). Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture. J. Cell Sci. 118(12): 2649--2660. (Export to RIS)
FlyBase ID	FBrf0187827
Publication Type	Research paper
PubMed ID	15928045
PubMed Abstract	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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Language of Publication	English
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Publication Type	Journal
Abbreviation	J. Cell Sci.
Title	Journal of Cell Science
Publication Year	1966-
ISBN/ISSN	0021-9533
Data from Reference
Alleles (12)
	Bsg^265.GMR Bsg⁰⁶²⁴³ Bsg^ex64 Bsg^k13638 Bsg^δ265 Ecol\lacZ^Bsg-k13638 mew^hs.PB mew^M6 Mmp2^W307stop Mmus\Bsg^GMR.PC mys^b45 mys^hs.PB
Constructs (2)
	P{GMR-Bsg.265} P{GMR-mBsg.C}
Genes (7)
	Bsg Ecol\lacZ elav mew Mmp2 Mmus\Bsg mys
Insertions (2)
	P{lacW}Bsg^k13638 P{PZ}Bsg⁰⁶²⁴³
Natural transposons (1)
	P-element