Densin-180: revised membrane topology, domain structure and phosphorylation status.
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.
Thalhammer
Agnes
A
UCL, Laboratory for Molecular Pharmacology, NPP, London, UK. a.thalhammer@ucl.ac.uk
Trinidad
Jonathan C
JC
Burlingame
Alma L
AL
Schoepfer
Ralf
R
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*
C504461:LRRC7 protein, human; D012795:Sialoglycoproteins