Densin-180 interacts with δ-catenin/neural plakophilin-related armadillo repeat protein at synapses

被引:68
作者
Izawa, I
Nishizawa, M
Ohtakara, K
Inagaki, M
机构
[1] Aichi Canc Ctr, Res Inst, Div Biochem, Chikusa Ku, Nagoya, Aichi 4648681, Japan
[2] Mie Univ, Sch Med, Dept Neurosurg, Tsu, Mie 5148507, Japan
关键词
D O I
10.1074/jbc.M110052200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Densin-180, a protein purified from the postsynaptic density fraction of the rat forebrain, is the founding member of a newly described family of proteins termed the LAP (leucine-rich repeats and PSD-95/Dlg-A/ZO-1 (PDZ) domains) family that plays essential roles in establishment of cell polarity. To identify Densin-180-binding proteins, we screened a yeast two-hybrid library using the carboxyl-terminal fragment of Densin-180 containing PDZ domain as bait, and we isolated delta-catenin/neural plakophilin-related armadillo repeat protein (NPRAP) as a Densin-180-interacting protein. delta-catenin/NPRAP, a member of the armadillo repeat family, is a nervous system-specific adherens junction protein originally discovered as an interactor with presenilin-1, a protein involved in Alzheimer's disease. Densin-180 PDZ domain binds the COOH terminus of delta-catenin/NPRAP containing the PDZ domain-binding sequence. Endogenous Densin-180 was co-immunoprecipitated with delta-catenin/NPRAP and N-cadherin. Although Densin-180 was reported to be a transmembrane protein, Densin-180 was not accessible to surface biotinylation in dissociated hippocampal neurons; hence Densin-180 may be a cytosolic protein. Densin-180 colocalized with delta-catenin/NPRAP at synapses in dissociated hippocampal neurons. We propose that Densin-180 is associated in vivo with delta-catenin/NPRAP and may be involved in organization of the synaptic cell-cell junction through interaction with the delta-catenin/NPRAP-N-cadherin complex.
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页码:5345 / 5350
页数:6
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