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Densin‐180: revised membrane topology, domain structure and phosphorylation status
Author(s) -
Thalhammer Agnes,
Trinidad Jonathan C.,
Burlingame Alma L.,
Schoepfer Ralf
Publication year - 2009
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2009.05951.x
Subject(s) - phosphorylation , topology (electrical circuits) , microbiology and biotechnology , intracellular , transmembrane protein , membrane topology , extracellular , scaffold protein , biology , signal transduction , transmembrane domain , chemistry , biophysics , membrane , biochemistry , receptor , mathematics , combinatorics
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.