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[Cancer Research 63, 2645-2648, May 15, 2003]
© 2003 American Association for Cancer Research

Tumor Biology

Prostate-specific Membrane Antigen Association with Filamin A Modulates Its Internalization and NAALADase Activity1

Gopalakrishnapillai Anilkumar, Sigrid A. Rajasekaran, Song Wang, Oliver Hankinson, Neil H. Bander2 and Ayyappan K. Rajasekaran3

Department of Pathology and Laboratory Medicine, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California 90095 [G. A., S. A. R., S. W., O. H., A. K. R.], and Department of Urology, Weill Medical College of Cornell University, New York, New York 10021 [N. H. B.]

Prostate-specific membrane antigen (PMSA) is an integral membrane protein highly expressed by prostate cancer cells. We reported previously that PSMA undergoes internalization via clathrin-coated pits (Liu et al., Cancer Res., 58: 4055–4060, 1998). In this study we demonstrate that filamin A, an actin cross-linking protein, associates with the cytoplasmic tail of PSMA and that this association of PSMA with filamin is involved in its localization to the recycling endosomal compartment. By ectopically expressing PSMA in filamin-negative and -positive cell lines, we additionally show that filamin binding to PSMA reduces the internalization rate of PSMA and its N-acelylated-{alpha} linked-acidic dipeptidase activity. These results suggest that filamin might be an important regulator of PSMA function.




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