title: Palmitoylation in the nucleus: a little fat around the edges.
abstract: Many proteins are post-translationally modified by lipid moieties such as palmitoyl or prenyl (e.g., farnesyl) groups, creating functional proteolipids. Lipid modifications share the property of increasing a protein's hydrophobicity and thus the propensity of that protein to associate with a membrane. These modifications are used to control the localization and activity of membrane-associated proteins. A well-recognized paradigm is farnesylation of the Ras GTPase that helps target this critical signaling protein to the plasma membrane.
authors.affiliation: Department of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI, USA. cfox@wisc.edu
authors.forename: Catherine A
authors.initials: CA
authors.lastname: Fox
authors.forename: Marc R
authors.initials: MR
authors.lastname: Gartenberg
mesh_terms: D000217:Acyltransferases / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism*; D006570:Heterochromatin / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D054878:Lipoylation; D017368:Protein Prenylation; D011499:Protein Processing, Post-Translational; D012097:Repressor Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D015398:Signal Transduction; D016615:Telomere / Q000378:metabolism; D034501:Telomere-Binding Proteins / Q000378:metabolism; D018631:ras Proteins / Q000378:metabolism
chemical_list: D006570:Heterochromatin; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D034501:Telomere-Binding Proteins; C074461:RIF1 protein, S cerevisiae; D000217:Acyltransferases; C511958:Pfa4 protein, S cerevisiae; D018631:ras Proteins