Huntingtin interacting protein 14 is an oncogenic human protein: Palmitoyl acyltransferase

Charles E. Ducker; Erin M. Stettler; Kevin J. French; John J. Upson; Charles D. Smith

doi:10.1038/sj.onc.1208171

Huntingtin interacting protein 14 is an oncogenic human protein: Palmitoyl acyltransferase

Charles E. Ducker, Erin M. Stettler, Kevin J. French, John J. Upson, Charles D. Smith

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96 Scopus citations

Abstract

Protein palmitoyltransferases (PATs) represent an exciting new target for anticancer drug design due to their pivotal roles in the subcellular localization of a number of oncogenes. We show that the Huntingtin interacting protein 14 (HIP14) is a PAT with a preference for the farnesyl-dependent palmitoylation motif found in H- and N-RAS. Characterization of HIP14 in mouse cells has revealed that it has the ability to induce colony formation in cell culture, anchorage-independent growth, and tumors in mice. Activity of the enzyme and its ability to transform cells is dependent on critical residues in the active site of the enzyme.

Original language	English (US)
Pages (from-to)	9230-9237
Number of pages	8
Journal	Oncogene
Volume	23
Issue number	57
DOIs	https://doi.org/10.1038/sj.onc.1208171
State	Published - Dec 9 2004

All Science Journal Classification (ASJC) codes

Molecular Biology
Genetics
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1038/sj.onc.1208171

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title = "Huntingtin interacting protein 14 is an oncogenic human protein: Palmitoyl acyltransferase",

abstract = "Protein palmitoyltransferases (PATs) represent an exciting new target for anticancer drug design due to their pivotal roles in the subcellular localization of a number of oncogenes. We show that the Huntingtin interacting protein 14 (HIP14) is a PAT with a preference for the farnesyl-dependent palmitoylation motif found in H- and N-RAS. Characterization of HIP14 in mouse cells has revealed that it has the ability to induce colony formation in cell culture, anchorage-independent growth, and tumors in mice. Activity of the enzyme and its ability to transform cells is dependent on critical residues in the active site of the enzyme.",

author = "Ducker, {Charles E.} and Stettler, {Erin M.} and French, {Kevin J.} and Upson, {John J.} and Smith, {Charles D.}",

note = "Funding Information: We thank Dwayne Dexter for assistance in obtaining the HIP14 clone. We are also grateful to Lynn Maines for his assistance in the preparation of the manuscript. This work was supported by NIH Grant No. R01 CA75248 to CDS.",

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doi = "10.1038/sj.onc.1208171",

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AU - Ducker, Charles E.

AU - Stettler, Erin M.

AU - French, Kevin J.

AU - Upson, John J.

AU - Smith, Charles D.

N1 - Funding Information: We thank Dwayne Dexter for assistance in obtaining the HIP14 clone. We are also grateful to Lynn Maines for his assistance in the preparation of the manuscript. This work was supported by NIH Grant No. R01 CA75248 to CDS.

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AB - Protein palmitoyltransferases (PATs) represent an exciting new target for anticancer drug design due to their pivotal roles in the subcellular localization of a number of oncogenes. We show that the Huntingtin interacting protein 14 (HIP14) is a PAT with a preference for the farnesyl-dependent palmitoylation motif found in H- and N-RAS. Characterization of HIP14 in mouse cells has revealed that it has the ability to induce colony formation in cell culture, anchorage-independent growth, and tumors in mice. Activity of the enzyme and its ability to transform cells is dependent on critical residues in the active site of the enzyme.

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Huntingtin interacting protein 14 is an oncogenic human protein: Palmitoyl acyltransferase

Abstract

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