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J Neurochem. 2009 Apr;109(2):297-302. doi: 10.1111/j.1471-4159.2009.05951.x. Epub 2009 Feb 2.

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

Author information

1
UCL, Laboratory for Molecular Pharmacology, NPP, London, UK. a.thalhammer@ucl.ac.uk

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.

PMID:
19187442
PMCID:
PMC2846389
DOI:
10.1111/j.1471-4159.2009.05951.x
[Indexed for MEDLINE]
Free PMC Article

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