Direct demonstration of NCAM cis-dimerization and inhibitory effect of palmitoylation using the BRET2 technique
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Direct demonstration of NCAM cis-dimerization and inhibitory effect of palmitoylation using the BRET2 technique. / Kulahin, Nikolaj; Grunnet, Lars Groth; Lundh, Morten; Christensen, Dan Ploug; Jorgensen, Rasmus; Heding, Anders; Billestrup, Nils; Berezin, Vladimir; Bock, Elisabeth; Mandrup-Poulsen, Thomas.
I: FEBS Letters, Bind 585, Nr. 1, 03.01.2011, s. 58-64.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Direct demonstration of NCAM cis-dimerization and inhibitory effect of palmitoylation using the BRET2 technique
AU - Kulahin, Nikolaj
AU - Grunnet, Lars Groth
AU - Lundh, Morten
AU - Christensen, Dan Ploug
AU - Jorgensen, Rasmus
AU - Heding, Anders
AU - Billestrup, Nils
AU - Berezin, Vladimir
AU - Bock, Elisabeth
AU - Mandrup-Poulsen, Thomas
N1 - Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
PY - 2011/1/3
Y1 - 2011/1/3
N2 - 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 (BRET(2)) 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.
AB - 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 (BRET(2)) 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.
KW - Animals
KW - COS Cells
KW - Cercopithecus aethiops
KW - Chemiluminescent Measurements
KW - Energy Transfer
KW - Green Fluorescent Proteins
KW - Humans
KW - Lipoylation
KW - Neural Cell Adhesion Molecules
KW - Protein Multimerization
KW - Recombinant Fusion Proteins
KW - Transfection
U2 - 10.1016/j.febslet.2010.11.043
DO - 10.1016/j.febslet.2010.11.043
M3 - Journal article
C2 - 21115007
VL - 585
SP - 58
EP - 64
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 1
ER -
ID: 33903163