p11 (S100A10), a member of a large family of S100 proteins, regulates the intracellular localization of metabotropic glutamate receptor 5 (mGluR5) and mGluR5 signaling, and is required for the antidepressant-like effect of mGluR5 antagonism. p11 is primarily localized in the cytoplasm and the plasma membrane (top panel). A dramatic redistribution of endogenous p11 from the cytoplasm to the plasma membrane was observed in human embryonic kidney 293 (HEK293) cells transfected with wild-type mGluR5 (middle panel). In contrast, when cells were transfected with the mutant form of mGluR5, which cannot bind to p11, p11 was partially present in the membrane but a significant portion remained in the cytoplasm (bottom panel). Bright-field imaging was performed to display the cell membrane and nucleus without labeling (first column). Color coding is as follows: red, immunofluorescence labeling of mGluR5 (second column); green, immunofluorescence labeling of p11 (third column). Merge of images of the first, second and third columns is displayed in the fourth column. Specific pixel-by-pixel colocalization of mGluR5 and p11 is represented with an intensity heat map in the fifth column. For more information on this topic, please refer to the article by Lee et al. on pages 1546–1556.
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