PMID- 16029167
OWN - NLM
STAT- MEDLINE
DCOM- 20060221
LR  - 20181201
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 392
IP  - Pt 1
DP  - 2005 Nov 15
TI  - Increase in cell-surface localization of parathyroid hormone receptor by 
      cytoskeletal protein 4.1G.
PG  - 75-81
AB  - The cell-surface localization of GPCRs (G-protein-coupled receptors) has emerged 
      as one of critical factors of the GPCR-mediated signal transduction. It has been 
      reported that the C-termini of GPCRs contain the sequences for sorting the 
      receptors to cell surface. In the present study, we have searched for proteins 
      that interact with the C-terminus of PTH (parathyroid hormone)/PTH-related 
      protein receptor (PTHR) by using the yeast two-hybrid system, and identified a 
      cytoskeletal protein 4.1G (generaltype 4.1 protein) as an interactant with the 
      C-terminus. Immunohistochemical study revealed that both PTHR and 4.1G were 
      co-localized on plasma membranes, when they were transiently expressed in COS-7 
      cells. When 4.1G or the C-terminal domain of 4.1G (4.1G-CTD), a dominant-negative 
      form of 4.1G, was co-expressed with PTHR in COS-7 cells, 4.1G, but not 4.1G-CTD, 
      facilitated the cell-surface localization of PTHR, determined by cell-surface 
      biotinylation assay. PTH-(1-34) caused phosphorylation of ERK 
      (extracellular-signal-regulated kinase) 1/2 in PTHR-expressed cells mainly 
      mediated through EGF (epidermal growth factor) receptor. The phosphorylation was 
      enhanced by the expression of 4.1G, but not 4.1G-CTD. PTH-(1-34) elevated [Ca2+]i 
      (intracellular Ca2+ concentration) independent of EGF receptor activation, and 
      the elevation was enhanced by the expression of 4.1G, but not 4.1G-CTD. These 
      data indicate that 4.1G facilitates the cell-surface localization of PTHR through 
      its interaction with the C-terminus of the receptor, resulting in the 
      potentiation of PTHR-mediated signal transduction.
FAU - Saito, Masaki
AU  - Saito M
AD  - Department of Cellular Signaling, Graduate School of Pharmaceutical Sciences, 
      Tohoku University, Aoba 6-3, Aramaki, Aoba-ku, Sendai 980-8578, Japan.
FAU - Sugai, Maki
AU  - Sugai M
FAU - Katsushima, Yuriko
AU  - Katsushima Y
FAU - Yanagisawa, Teruyuki
AU  - Yanagisawa T
FAU - Sukegawa, Jun
AU  - Sukegawa J
FAU - Nakahata, Norimichi
AU  - Nakahata N
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptor, Parathyroid Hormone, Type 1)
RN  - 0 (erythrocyte membrane band 4.1 protein)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.11.25 (MAP Kinase Kinase Kinases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Calcium/metabolism
MH  - Cell Line
MH  - Cell Membrane/metabolism
MH  - Cytoskeletal Proteins/*metabolism
MH  - ErbB Receptors/metabolism
MH  - Gene Expression Regulation
MH  - Humans
MH  - MAP Kinase Kinase Kinases/metabolism
MH  - Membrane Proteins/*metabolism
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Protein Transport
MH  - Receptor, Parathyroid Hormone, Type 1/*metabolism
MH  - Two-Hybrid System Techniques
PMC - PMC1317666
EDAT- 2005/07/21 09:00
MHDA- 2006/02/24 09:00
PMCR- 2006/05/15
CRDT- 2005/07/21 09:00
PHST- 2005/07/21 09:00 [pubmed]
PHST- 2006/02/24 09:00 [medline]
PHST- 2005/07/21 09:00 [entrez]
PHST- 2006/05/15 00:00 [pmc-release]
AID - BJ20050618 [pii]
AID - bj3920075 [pii]
AID - 10.1042/BJ20050618 [doi]
PST - ppublish
SO  - Biochem J. 2005 Nov 15;392(Pt 1):75-81. doi: 10.1042/BJ20050618.