title: Tyrosinase maturation through the mammalian secretory pathway: bringing color to life.
abstract: Tyrosinase has been extensively utilized as a model substrate to study the maturation of glycoproteins in the mammalian secretory pathway. The visual nature of its enzymatic activity (melanin production) has facilitated the identification and characterization of the proteins that assist it becoming a functional enzyme, localized to its proper cellular location. Here, we review the steps involved in the maturation of tyrosinase from when it is first synthesized by cytosolic ribosomes until the mature protein reaches its post-Golgi residence in the melanosomes. These steps include protein processing, covalent modifications, chaperone binding, oligomerization, and trafficking. The disruption of any of these steps can lead to a wide range of pigmentation disorders.
authors.affiliation: Program in Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.
authors.forename: Ning
authors.initials: N
authors.lastname: Wang
authors.forename: Daniel N
authors.initials: DN
authors.lastname: Hebert
mesh_terms: D001692:Biological Transport / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism; D006801:Humans; D008543:Melanins / Q000096:biosynthesis; D008544:Melanocytes / Q000166:cytology / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D015394:Molecular Structure; D014442:Monophenol Monooxygenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals
chemical_list: D008543:Melanins; D018832:Molecular Chaperones; D021382:Protein Sorting Signals; D014442:Monophenol Monooxygenase