AMSH regulates calcium-sensing receptor signaling through direct interactions.
Calcium-sensing receptor (CaR) activates intracellular pathways controlling calcium homeostasis. CaR carboxyl-terminal mutants associated with metabolic diseases suggest that unidentified proteins interact with the carboxyl-terminal region of this receptor. To address this possibility, we screened for CaR-interacting proteins using the carboxyl terminus of CaR (CaRDelta895-1075 deletion mutant). We identified AMSH, an ubiquitin isopeptidase, as a CaR-interacting partner. AMSH caused a decrease on the signaling properties of wild-type and mutant CaR. Our results indicate that AMSH, which has been recently characterized as a regulator of the endosomal sorting of epidermal growth factor receptor, represents a novel modulator of CaR signaling.
Herrera-Vigenor
Francisco
F
Department of Cell Biology, CINVESTAV-IPN Apartado postal 14-740, México DF 07000, Mexico.
Hernández-García
Ricardo
R
Valadez-Sánchez
Margarita
M
Vázquez-Prado
José
J
Reyes-Cruz
Guadalupe
G
D000595:Amino Acid Sequence; D002478:Cells, Cultured; D010450:Endopeptidases / Q000502:physiology*; D056827:Endosomal Sorting Complexes Required for Transport; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology; D044169:Receptors, Calcium-Sensing / Q000235:genetics / Q000502:physiology*; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology*; D043222:Ubiquitin Thiolesterase
D056827:Endosomal Sorting Complexes Required for Transport; D010446:Peptide Fragments; D044169:Receptors, Calcium-Sensing; C486696:STAMBP protein, human; D010450:Endopeptidases; D043222:Ubiquitin Thiolesterase