Post-translational modification of proteins by attachment of palmitate serves as a mechanism to regulate protein localization and function in both normal and malignant cells. Given the essential role that palmitoylation plays in cancer cell signaling, approaches that target palmitoylated proteins and palmitoyl acyltransferases (PATs) have the potential for therapeutic intervention in cancer. Highlighted here are recent advances in understanding the importance of protein palmitoylation in tumorigenic pathways. A new study has uncovered palmitoylation sites within the epidermal growth factor receptor that regulate receptor trafficking, signaling and sensitivity to tyrosine kinase inhibitors. Global data analysis from nearly 150 cancer studies reveals genomic alterations in several PATs that may account for their ability to function as tumor suppressors or oncogenes. Selective inhibitors have recently been developed that target hedgehog acyltransferase (Hhat) and Porcupine (Porcn), the acyltransferases that modify hedgehog and Wnt proteins, respectively. These inhibitors, coupled with targeted knockdown of Hhat and Porcn, reveal the essential functions of fatty acylation of secreted morphogens in a wide variety of human tumors.
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April 2017
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Cover Image
This artistic rendition shows an Atomic Force Microscopy tip probing the mechanics of an individual virus particle. The colour scale of the particle indicates the deformation and stress of the viral shell obtained with Finite Element Analysis. The applied force is monitored by focusing a laser beam at the end of the microcantilever. For more information please see study by Moreno-Madrid et al. in this issue, pages 499–511. Image provided by Pedro De Pablo.
Review Article|
April 13 2017
Palmitoylation of proteins in cancer
Marilyn D. Resh
1Cell Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, Box 143, New York, NY 10065, U.S.A.
Correspondence: Marilyn D. Resh (reshm@mskcc.org)
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Publisher: Portland Press Ltd
Received:
December 19 2016
Revision Received:
January 30 2017
Accepted:
February 06 2017
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (2): 409–416.
Article history
Received:
December 19 2016
Revision Received:
January 30 2017
Accepted:
February 06 2017
Citation
Marilyn D. Resh; Palmitoylation of proteins in cancer. Biochem Soc Trans 15 April 2017; 45 (2): 409–416. doi: https://doi.org/10.1042/BST20160233
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