Palmitoylation of proteins in cancer Journal Article


Author: Resh, M. D.
Article Title: Palmitoylation of proteins in cancer
Abstract: 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. © 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society.
Keywords: review; nonhuman; protein targeting; epidermal growth factor receptor; sonic hedgehog protein; protein; cancer inhibition; cell polarity; wnt protein; acyltransferase; palmitoylation; wnt signaling pathway; human; priority journal; malignant neoplasm
Journal Title: Biochemical Society Transactions
Volume: 45
Issue: 2
ISSN: 0300-5127
Publisher: Portland Press Ltd  
Date Published: 2017-04-15
Start Page: 409
End Page: 416
Language: English
DOI: 10.1042/bst20160233
PUBMED: 28408481
PROVIDER: scopus
DOI/URL:
Notes: Review -- Export Date: 2 June 2017 -- Source: Scopus
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  1. Marilyn D Resh
    101 Resh