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Interactions of the Dopamine D2 Receptor with the Calcium‐Binding Protein S100B
Author(s) -
Neve Kim A,
Liu Yong
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.726.2
Subject(s) - dopamine receptor d2 , receptor , hek 293 cells , microbiology and biotechnology , enzyme linked receptor , 5 ht5a receptor , dopamine receptor , chemistry , biology , biochemistry
S100B is a calcium‐binding protein with numerous regulatory activities in the mammalian brain. Using a bacterial two‐hybrid assay, we have identified a novel interaction between S100B and the third cytoplasmic loop of the dopamine D2 receptor (D2‐IC3). The binding of S100B to D2‐IC3 was confirmed using a polyHis pull‐down assay. The binding of heterologous S100B to full‐length D2 receptor in HEK293 cells, and of endogenous S100B to endogenous D2 receptor in the rat neostriatum, was demonstrated by co‐precipitation. A putative S100B binding motif is near the N‐terminus of D2‐IC3. Although S100B is considered a glial protein, S100B expression was detected in microtubule‐associated protein‐2 (MAP2) expressing neurons in neostriatal cultures. Expression of S100B in HEK293 cells also stably expressing the D2 receptor significantly increased D2 receptor stimulation of extracellular signal‐regulated kinases (ERKs), while causing little change in NGF‐stimulated activation of ERKs, and also potentiated D2 receptor inhibition of cyclic AMP accumulation. Taken together, these fundings suggest that the interaction of S100B with the D2 dopamine receptor enhances D2 receptor signaling. (MH045372 and VA Merit Review)