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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.

SUBMITTER: Thalhammer A 

PROVIDER: S-EPMC2846389 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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Densin-180: revised membrane topology, domain structure and phosphorylation status.

Thalhammer Agnes A   Trinidad Jonathan C JC   Burlingame Alma L AL   Schoepfer Ralf R  

Journal of neurochemistry 20090202 2


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 i  ...[more]

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