Internalization and recycling properties of neurotensin receptors.
The targeting, internalization and recycling of membrane receptors in response to extracellular ligands involve a series of molecular mechanisms which are beginning to be better understood. The receptor-dependent internalization of neurotensin has been widely investigated using endogenous or heterologous receptor expression systems. This review focuses on the general properties of neurotensin sequestration and on the characterization of the receptors involved in this process.
Mazella
Jean
J
Institut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 6097 du Centre National de la Recherche Scientifique, et de l'Université de Nice-Sophia Antipolis, Sophia Antipolis, 06560 Valbonne, France. mazella@ipmc.cnrs.fr
Vincent
Jean-Pierre
JP
D033942:Adaptor Proteins, Vesicular Transport; D000818:Animals; D001693:Biological Transport, Active; D004705:Endocytosis; D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism; D008959:Models, Neurological; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009496:Neurotensin / Q000378:metabolism; D018028:Receptors, Neurotensin / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D000099183:Sortilin
D033942:Adaptor Proteins, Vesicular Transport; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D009496:Neurotensin; D018028:Receptors, Neurotensin; D011994:Recombinant Proteins; D000099183:Sortilin; C114036:neurotensin type 1 receptor