TY - JOUR
T1 - PTH/PTH-related protein receptor interacts directly with Tctex-1 through its COOH terminus
AU - Sugai, Maki
AU - Saito, Masaki
AU - Sukegawa, Izumi
AU - Katsushima, Yuriko
AU - Kinouchi, Yoshitaka
AU - Nakahata, Norimichi
AU - Shimosegawa, Tooru
AU - Yanagisawa, Teruyuki
AU - Sukegawa, Jun
PY - 2003/11/7
Y1 - 2003/11/7
N2 - 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.
AB - 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.
KW - Dynein
KW - Internalization
KW - PTH/PTHrP receptor
KW - Tctex-1
UR - http://www.scopus.com/inward/record.url?scp=0142122528&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0142122528&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2003.09.157
DO - 10.1016/j.bbrc.2003.09.157
M3 - Article
C2 - 14575690
AN - SCOPUS:0142122528
SN - 0006-291X
VL - 311
SP - 24
EP - 31
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -