Importance of a N-terminal aspartate in the internalization of the neuropeptide Y Y2 receptor.
With human neuropeptide Y Y2 receptor expressed in the Chinese hamster ovary (CHO) cells, the Asp35Ala mutation, and especially the change of Pro34Asp35 to Ala34Ala35, decrease the compartmentalization and strongly accelerate internalization of the receptor. These changes are not associated with alterations in agonist affinity, G-protein interaction, dimerization, or level of expression of the mutated receptors relative to the wildtype receptor. The proline-flanked aspartate in the N-terminal extracellular segment of the neuropeptide Y Y2 receptor thus apparently has a large role in anchoring and compartmentalization of the receptor. However, the Pro34Ala mutation does not significantly affect the embedding and cycling of the receptor.
Parker
Steven L
SL
Department of Pharmacology, University of Tennessee Health Science Center, Memphis, TN 38163, USA. stevenleonardparker@msn.com
Parker
Michael S
MS
Wong
Ying Y
YY
Sah
Renu
R
Balasubramaniam
Ambikaipakan
A
Sallee
Floyd
F
D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000502:physiology*; D001665:Binding Sites; D016466:CHO Cells; D006224:Cricetinae; D003412:Cricetulus; D017931:DNA Primers; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D017476:Receptors, Neuropeptide Y / Q000235:genetics* / Q000378:metabolism*
D017931:DNA Primers; D017476:Receptors, Neuropeptide Y; C095889:neuropeptide Y2 receptor; D001224:Aspartic Acid; D019204:GTP-Binding Proteins