PTH/PTH-related protein receptor interacts directly with Tctex-1 through its COOH terminus
| Autor: | Teruyuki Yanagisawa, Norimichi Nakahata, Yoshitaka Kinouchi, Tooru Shimosegawa, Jun Sukegawa, Yuriko Katsushima, Maki Sugai, Izumi Sukegawa, Masaki Saito |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Cytoplasm
media_common.quotation_subject Amino Acid Motifs Molecular Sequence Data Biophysics Plasma protein binding Biology Kidney Biochemistry T-Complex Genome Region Protein structure GTP-Binding Proteins Consensus Sequence Humans Amino Acid Sequence Binding site Receptor Internalization Molecular Biology Peptide sequence G protein-coupled receptor media_common Receptor Parathyroid Hormone Type 1 t-Complex Genome Region Brain Chemistry Binding Sites Brain Nuclear Proteins Cell Biology Carbon Dioxide Molecular biology Peptide Fragments Protein Structure Tertiary Microtubule Proteins Microtubule-Associated Proteins Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 311(1) |
| ISSN: | 0006-291X |
| Popis: | COOH-terminal cytoplasmic domains of G protein-coupled receptors (GPCRs) have been shown to carry determinants that control their cell surface localization, internalization, and recycling. In attempts to seek cellular proteins that mediate these processes of PTH/PTH-related protein receptor (PTHR), one of the class B GPCRs, we have found that Tctex-1, a 14kDa light chain of cytoplasmic dynein motor complex, interacts with the COOH-terminal tail of the receptor. A 34-amino-acid stretch of the receptor responsible for binding to Tctex-1 has a bipartite structure consisting of a motif previously implicated in binding of some proteins to Tctex-1 and a putative new consensus sequence. Site-directed mutations or a 20-amino-acid deletion in the bipartite consensus binding sequence abolished the association of the PTHR COOH terminus with Tctex-1 in vitro. A GFP-fused mutant PTHR impaired in binding to Tctex-1 expressed in MDCK cells showed a decreased rate of internalization in response to PTH compared to that of the wild type. |
| Databáze: | OpenAIRE |
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