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Binding of pro-prion to filamin A: by design or an unfortunate blunder

Oncogene volume 29, pages 5329–5345 (2010)Cite this article

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Abstract

Over the last decades, cancer research has focused on tumor suppressor genes and oncogenes. Genes in other cellular pathways has received less attention. Between 0.5% to 1% of the mammalian genome encodes for proteins that are tethered on the cell membrane via a glycosylphosphatidylinositol (GPI)-anchor. The GPI modification pathway is complex and not completely understood. Prion (PrP), a GPI-anchored protein, is infamous for being the only normal protein that when misfolded can cause and transmit a deadly disease. Though widely expressed and highly conserved, little is known about the functions of PrP. Pancreatic cancer and melanoma cell lines express PrP. However, in these cell lines the PrP exists as a pro-PrP as defined by retaining its GPI anchor peptide signal sequence (GPI-PSS). Unexpectedly, the GPI-PSS of PrP has a filamin A (FLNA) binding motif and binds FLNA. FLNA is a cytolinker protein, and an integrator of cell mechanics and signaling. Binding of pro-PrP to FLNA disrupts the normal FLNA functions. Although normal pancreatic ductal cells lack PrP, about 40% of patients with pancreatic ductal cell adenocarcinoma express PrP in their cancers. These patients have significantly shorter survival time compared with patients whose cancers lack PrP. Pro-PrP is also detected in melanoma in situ but is undetectable in normal melanocyte, and invasive melanoma expresses more pro-PrP. In this review, we will discuss the underlying mechanisms by which binding of pro-PrP to FLNA disrupts normal cellular physiology and contributes to tumorigenesis, and the potential mechanisms that cause the accumulation of pro-PrP in cancer cells.

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Acknowledgements

We thank all the collaborators who have contributed to these studies, and Pearl Ling for careful reading of the paper, suggestion and editorial assistant. Start-up funds from the Department of Pathology to WX. Supported by R21-CA133559-01 from NIH and a pilot Grant from SDRC#5P30AR039750 from NIH.

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  1. Department of Pathology, School of Medicine, Case Western Reserve University, Cleveland, OH, USA

    C Li & M-S Sy

  2. Department of Pathology, University Hospital Case Medical Center, Cleveland, OH, USA

    W Xin

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  3. M-S Sy
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Li, C., Xin, W. & Sy, MS. Binding of pro-prion to filamin A: by design or an unfortunate blunder. Oncogene 29, 5329–5345 (2010). https://doi.org/10.1038/onc.2010.307

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