期刊
FEBS LETTERS
卷 585, 期 1, 页码 58-64出版社
WILEY
DOI: 10.1016/j.febslet.2010.11.043
关键词
Neural cell adhesion molecule; Homophilic binding; cis-interaction; Bioluminescence resonance energy transfer; Palmitoylation
资金
- Danish Research Council for Independent Research, Medical Sciences
- Novo Nordisk Foundation
Biological activity of the neural cell adhesion molecule (NCAM) depends on both adhesion and activation of intra-cellular signaling. Based on in vitro experiments with truncated extra-cellular domains, several models describing homophilic NCAM trans- and cis-interactions have been proposed. However, cis-dimerization in living cells has not been shown directly and the role of the cytoplasmic part in NCAM dimerization is poorly understood. Here, we used the bioluminescence resonance energy transfer (BRET2) technique to directly demonstrate that full-length NCAM cis-homodimerizes in living cells. Based on BRET(2)50 values we suggest that the intra-cellular part of NCAM inhibits cis-dimerization, an effect mainly dependent on the palmitoylation sites. Structured summary: MINT-8071463:NCAM140 (uniprotkb:P13591-1) physically interacts (MI:0915) with NCAM140 (uniprotkb:P13591-1) by bioluminescence resonance energy transfer (MI:0012) MINT-8071506:NCAM180 (genbank_protein_gi:119587605) physically interacts (MI:0915) with NCAM180 (genbank_protein_gi:119587605) by bioluminescence resonance energy transfer (MI:0012) MINT-8071483:NCAM140 (uniprotkb:P13591-1) physically interacts (MI:0915) with NCAM140 (uniprotkb:P13591-1) by competition binding (MI:0405) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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