Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase.
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.
Department of Pharmacology, H078, Penn State College of Medicine, 500 University Drive Hershey, PA 17033, USA.
Charles E
CE
Ducker
Erin M
EM
Stettler
Kevin J
KJ
French
John J
JJ
Upson
Charles D
CD
Smith
D000217:Acyltransferases; D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000502:physiology*; D002471:Cell Transformation, Neoplastic; D017931:DNA Primers; D005260:Female; D006801:Humans; D051379:Mice; D016688:Mice, Inbred NOD; D016513:Mice, SCID; D041681:NIH 3T3 Cells; D009419:Nerve Tissue Proteins / Q000502:physiology*
D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; D017931:DNA Primers; D009419:Nerve Tissue Proteins; D000217:Acyltransferases; C473038:ZDHHC17 protein, human