Imperial College London

DrAylinHanyaloglu

Faculty of MedicineDepartment of Metabolism, Digestion and Reproduction

Reader in Cell Biology
 
 
 
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Contact

 

+44 (0)20 7594 2128a.hanyaloglu Website

 
 
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Assistant

 

Miss Kiran Dosanjh +44 (0)20 7594 2176

 
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Location

 

2009Institute of Reproductive and Developmental BiologyHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Sposini:2014:10.1016/j.mce.2014.10.024,
author = {Sposini, S and Caltabiano, G and Hanyaloglu, AC and Miele, R},
doi = {10.1016/j.mce.2014.10.024},
journal = {Molecular and Cellular Endocrinology},
pages = {362--372},
title = {Identification of transmembrane domains that regulate spatial arrangements and activity of prokineticin receptor 2 dimers},
url = {http://dx.doi.org/10.1016/j.mce.2014.10.024},
volume = {399},
year = {2014}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The chemokine prokineticin 2 (PK2) activates its cognate G protein-coupled receptor (GPCR) PKR2 to elicit various downstream signaling pathways involved in diverse biological processes. Many GPCRs undergo dimerization that can modulate a number of functions including membrane delivery and signal transduction. The aim of this study was to elucidate the interface of PKR2 protomers within dimers by analyzing the ability of PKR2 transmembrane (TM) deletion mutants to associate with wild type (WT) PKR2 in yeast using co-immunoprecipitation and mammalian cells using bioluminescence resonance energy transfer. Deletion of TMs 5-7 resulted in a lack of detectable association with WT PKR2, but could associate with a truncated mutant lacking TMs 6-7 (TM1-5). Interestingly, TM1-5 modulated the distance, or organization, between protomers and positively regulated Gαs signaling and surface expression of WT PKR2. We propose that PKR2 protomers form type II dimers involving TMs 4 and 5, with a role for TM5 in modulation of PKR2 function.
AU - Sposini,S
AU - Caltabiano,G
AU - Hanyaloglu,AC
AU - Miele,R
DO - 10.1016/j.mce.2014.10.024
EP - 372
PY - 2014///
SN - 1872-8057
SP - 362
TI - Identification of transmembrane domains that regulate spatial arrangements and activity of prokineticin receptor 2 dimers
T2 - Molecular and Cellular Endocrinology
UR - http://dx.doi.org/10.1016/j.mce.2014.10.024
UR - http://hdl.handle.net/10044/1/31246
VL - 399
ER -