%0 Journal Article %1 perron_nts2_2007 %A Perron, Amélie %A Sharif, Nadder %A Sarret, Philippe %A Stroh, Thomas %A Beaudet, Alain %D 2007 %J Biochemical and Biophysical Research Communications %K Animals Cercopithecus_aethiops Confocal Dimerization Microscopy Neurotensin Protein_Transport Rats Receptors Transfection {COS}_Cells {Down-Regulation} {MAP}_Kinase_Signaling_System %N 3 %P 582--590 %R 10.1016/j.bbrc.2006.12.062 %T NTS2 modulates the intracellular distribution and trafficking of NTS1 via heterodimerization %U http://www.ncbi.nlm.nih.gov/pubmed/17188644 %V 353 %X Neurotensin (NT) receptors NTS1 and NTS2 are known to display considerable distributional overlap in mammalian central nervous system (CNS). Using co-immunoprecipitation approaches, we demonstrated here that NTS1 forms constitutive heterodimers with NTS2 in transfected COS-7 cells. We also showed that co-expression of NTS2 with NTS1 markedly decreases the cell surface density of NTS1 without affecting ERK1/2 MAPK activity or NT-induced NTS1 internalization. However, radioligand-binding studies indicated that upon prolonged NT stimulation, cell surface NTS1 receptors are more resistant to down-regulation in cells co-expressing NTS1 and NTS2 than in cells expressing NTS1 alone. Taken together, these data suggest that NTS1/NTS2 heterodimerization affects the intracellular distribution and trafficking of NTS1 by making it more similar to that of NTS2 as witnessed in cells expressing NTS2 alone. NTS1/NTS2 heterodimerization might therefore represent an additional mechanism in the regulation of NT-triggered responses mediated by NTS1 and NTS2 receptors.

@article{perron_nts2_2007, abstract = {Neurotensin {(NT)} receptors {NTS1} and {NTS2} are known to display considerable distributional overlap in mammalian central nervous system {(CNS).} Using co-immunoprecipitation approaches, we demonstrated here that {NTS1} forms constitutive heterodimers with {NTS2} in transfected {COS-7} cells. We also showed that co-expression of {NTS2} with {NTS1} markedly decreases the cell surface density of {NTS1} without affecting {ERK1/2} {MAPK} activity or {NT-induced} {NTS1} internalization. However, radioligand-binding studies indicated that upon prolonged {NT} stimulation, cell surface {NTS1} receptors are more resistant to down-regulation in cells co-expressing {NTS1} and {NTS2} than in cells expressing {NTS1} alone. Taken together, these data suggest that {NTS1/NTS2} heterodimerization affects the intracellular distribution and trafficking of {NTS1} by making it more similar to that of {NTS2} as witnessed in cells expressing {NTS2} alone. {NTS1/NTS2} heterodimerization might therefore represent an additional mechanism in the regulation of {NT-triggered} responses mediated by {NTS1} and {NTS2} receptors.}, added-at = {2011-08-03T17:38:07.000+0200}, author = {Perron, Amélie and Sharif, Nadder and Sarret, Philippe and Stroh, Thomas and Beaudet, Alain}, biburl = {https://www.bibsonomy.org/bibtex/2b50c86088193b21135611752f86ef00a/crc_chus}, doi = {10.1016/j.bbrc.2006.12.062}, interhash = {ff879c32d59578ae9f5a67a0b0a369fc}, intrahash = {b50c86088193b21135611752f86ef00a}, issn = {{0006-291X}}, journal = {Biochemical and Biophysical Research Communications}, keywords = {Animals Cercopithecus_aethiops Confocal Dimerization Microscopy Neurotensin Protein_Transport Rats Receptors Transfection {COS}_Cells {Down-Regulation} {MAP}_Kinase_Signaling_System}, month = feb, note = {{PMID:} 17188644}, number = 3, pages = {582--590}, timestamp = {2011-08-03T20:52:18.000+0200}, title = {{NTS2} modulates the intracellular distribution and trafficking of {NTS1} via heterodimerization}, url = {http://www.ncbi.nlm.nih.gov/pubmed/17188644}, volume = 353, year = 2007 }