title: A CULLINary ride across the secretory pathway: more than just secretion.
abstract: Mulitmeric cullin-RING ubiquitin ligases (CRLs) represent the largest class of ubiquitin ligases in eukaryotes. However, most CRL ubiquitylation pathways remain uncharacterized. CRLs control a myriad of functions by catalyzing mono- or poly-ubiquitylation of target proteins. Recently, novel CRLs have been identified along the secretory pathway where they modify substrates involved in diverse cellular processes such as vesicle coat assembly and cell cycle progression. This review discusses our current understanding of CRL ubiquitylation within the secretory pathway, with special emphasis on the emerging role of the Golgi as a ubiquitylation platform. CRLs are also implicated in endosome function, where their specific roles are less well understood.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. Electronic address: alulopez@stanford.edu.
authors.forename: Albert
authors.initials: A
authors.lastname: Lu
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. Electronic address: pfeffer@stanford.edu.
authors.forename: Suzanne R
authors.initials: SR
authors.lastname: Pfeffer
mesh_terms: D000818:Animals; D044842:Cullin Proteins / Q000378:metabolism*; D011992:Endosomes / Q000378:metabolism / Q000502:physiology; D006056:Golgi Apparatus / Q000378:metabolism / Q000502:physiology; D006801:Humans; D021381:Protein Transport / Q000502:physiology*; D055571:Secretory Pathway / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D054875:Ubiquitination / Q000502:physiology
chemical_list: D044842:Cullin Proteins; D044767:Ubiquitin-Protein Ligases
keywords: Golgi complex; cullin proteins; cullin-RING ligases; post-translational modification; ubiquitylation