title: Recent advances in protein prenyltransferases: substrate identification, regulation, and disease interventions.
abstract: Protein post-translational modifications increase the functional diversity of the proteome by covalently adding chemical moieties onto proteins thereby changing their activation state, cellular localization, interacting partners, and life cycle. Lipidation is one such modification that enables membrane association of naturally cytosolic proteins. Protein prenyltransferases irreversibly install isoprenoid units of varying length via a thioether linkage onto proteins that exert their cellular activity at membranes. Substrates of prenyltransferases are involved in countless signaling pathways and processes within the cell. Identification of new prenylation substrates, prenylation pathway regulators, and dynamic trafficking of prenylated proteins are all avenues of intense, ongoing research that are challenging, exciting, and have the potential to significantly advance the field in the near future.
authors.affiliation: Chemical Biology Program, University of Michigan, Ann Arbor, MI 48109, United States.
authors.forename: Elaina A
authors.initials: EA
authors.lastname: Zverina
authors.forename: Corissa L
authors.initials: CL
authors.lastname: Lamphear
authors.forename: Elia N
authors.initials: EN
authors.lastname: Wright
authors.forename: Carol A
authors.initials: CA
authors.lastname: Fierke
mesh_terms: D000818:Animals; D001424:Bacterial Infections / Q000201:enzymology / Q000378:metabolism; D018407:Bacterial Physiological Phenomena; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D006801:Humans; D009369:Neoplasms / Q000201:enzymology; D017368:Protein Prenylation; D013379:Substrate Specificity
chemical_list: D004122:Dimethylallyltranstransferase