Physical association of GPR54 C-terminal with protein phosphatase 2A.
Publication/Presentation Date
12-26-2008
Abstract
KiSS1 was discovered as a metastasis suppressor gene and subsequently found to encode kisspeptins (KP), ligands for a G protein coupled receptor (GPCR), GPR54. This ligand-receptor pair was later shown to play a critical role in the neuro-endocrine regulation of puberty. The C-terminal cytoplasmic (C-ter) domain of GPR54 contains a segment rich in proline and arginine residues that corresponds to the primary structure of four overlapping SH3 binding motifs. Yeast two hybrid experiments identified the catalytic subunit of protein phosphatase 2A (PP2A-C) as an interacting protein. Pull-down experiments with GST fusion proteins containing the GPR54 C-ter confirmed binding to PP2A-C in cell lysates and these complexes contained phosphatase activity. The proline arginine rich segment is necessary for these interactions. The GPR54 C-ter bound directly to purified recombinant PP2A-C, indicating the GPR54 C-ter may form complexes involving the catalytic subunit of PP2A that regulate phosphorylation of critical signaling intermediates.
Volume
377
Issue
4
First Page
1067
Last Page
1071
ISSN
1090-2104
Published In/Presented At
Evans, B. J., Wang, Z., Mobley, L., Khosravi, D., Fujii, N., Navenot, J. M., & Peiper, S. C. (2008). Physical association of GPR54 C-terminal with protein phosphatase 2A. Biochemical and biophysical research communications, 377(4), 1067–1071. https://doi.org/10.1016/j.bbrc.2008.10.108
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
18977201
Department(s)
Administration and Leadership
Document Type
Article