title: Coaxing the LDL receptor family into the fold.
abstract: Low-density-lipoprotein (LDL) receptor family members control diverse developmental and physiological pathways. In this issue of Cell, both Culi and Mann and Hsieh et al. report on Boca/MESD, a highly conserved chaperone required for transport of LDLR family proteins to the cell surface. Together with recent insights into the atomic structure of the LDL receptor, they shed new light on the synthesis and trafficking of this important class of multifunctional receptors.
authors.affiliation: Department of Molecular Genetics, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA. joachim.herz@utsouthwestern.edu
authors.forename: Joachim
authors.initials: J
authors.lastname: Herz
authors.forename: Peter
authors.initials: P
authors.lastname: Marschang
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D017510:Protein Folding; D017434:Protein Structure, Tertiary / Q000502:physiology; D021381:Protein Transport / Q000502:physiology; D011973:Receptors, LDL / Q000096:biosynthesis*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D018832:Molecular Chaperones; D011973:Receptors, LDL