41 351

Cited 0 times in

The alpha subunit of Go interacts with promyelocytic leukemia zinc finger protein and modulates its functions.

Authors
Won, JH; Park, JS; Ju, HH; Kim, S; Suh-Kim, H; Ghil, SH
Citation
Cellular signalling, 20(5):884-891, 2008
Journal Title
Cellular signalling
ISSN
0898-65681873-3913
Abstract
Heterotrimeric GTP-binding proteins (G proteins) mediate signal transduction generated by neurotransmitters and hormones. Go, a member of the Go/Gi family, is the most abundant heterotrimeric G protein in the brain. Most mechanistic analyses on Go activation demonstrate that its action is mediated by the Gbetagamma dimer; downstream effectors for its alpha subunit (Goalpha) have not been clearly defined. Here, we employ the yeast two-hybrid system to screen for Goalpha-interacting partners in a cDNA library from human fetal brain. The transcription factor promyelocytic leukemia zinc finger protein (PLZF) specifically bound to Goalpha. Interactions between PLZF and Goalpha were confirmed using in vitro and in vivo affinity binding assays. Activated Goalpha interacted directly with PLZF, and enhanced its function as a transcriptional and cell growth suppressor. Notably, PLZF activity was additionally promoted by the Go/ialpha-coupled cannabinoid receptor (CB) in HL60 cells endogenously expressing CB and PLZF. These results collectively suggest that Goalpha modulates the function of PLZF via direct interactions. Our novel findings provide insights into the diverse cellular roles of Goalpha and its coupled receptor.
MeSH terms
AnimalsBase SequenceCell LineCell ProliferationDNA Primers/geneticsGTP-Binding Protein alpha Subunits, Gi-Go/geneticsGTP-Binding Protein alpha Subunits, Gi-Go/metabolism*Gene LibraryHumansKruppel-Like Transcription Factors/geneticsKruppel-Like Transcription Factors/metabolism*MiceMultiprotein ComplexesProtein BindingReceptors, Cannabinoid/metabolismRecombinant Fusion Proteins/geneticsRecombinant Fusion Proteins/metabolismSignal TransductionTwo-Hybrid System Techniques
DOI
10.1016/j.cellsig.2007.12.022
PMID
18262754
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Anatomy
AJOU Authors
김, 소연서, 해영
Full Text Link
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse