title: Densin-180: revised membrane topology, domain structure and phosphorylation status.
abstract: Densin-180 is a core component of post-synaptic densities, the highly complex molecular assemblies that mediate signaling between neuronal cells. It is a multi-domain scaffold protein characterized by multiple leucine-rich repeat domains plus a single Psd95/Discs large/Zona occludens-1 domain. In its original topology model a single transmembrane segment was proposed with an extracellular N-terminus and an intracellular C-terminus. However, recently discovered in vivo phosphorylation sites are incompatible with this topology. Here, we discuss an all-intracellular and membrane-associated localization of Densin-180 that is consistent with and supported by all the latest experimental data. This revised topology which now includes also a phosphorylation-rich area will have deciding influence on future research involving Densin-180 and its signaling.
authors.affiliation: UCL, Laboratory for Molecular Pharmacology, NPP, London, UK. a.thalhammer@ucl.ac.uk
authors.forename: Agnes
authors.initials: A
authors.lastname: Thalhammer
authors.forename: Jonathan C
authors.initials: JC
authors.lastname: Trinidad
authors.forename: Alma L
authors.initials: AL
authors.lastname: Burlingame
authors.forename: Ralf
authors.initials: R
authors.lastname: Schoepfer
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007425:Intracellular Membranes / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary / Q000502:physiology; D012795:Sialoglycoproteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C504461:LRRC7 protein, human; D012795:Sialoglycoproteins