|
|
|
|
| LEADER |
01000caa a22002652 4500 |
| 001 |
NLM234263024 |
| 003 |
DE-627 |
| 005 |
20240506231927.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231224s2014 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1021/la404055a
|2 doi
|
| 028 |
5 |
2 |
|a pubmed24n1399.xml
|
| 035 |
|
|
|a (DE-627)NLM234263024
|
| 035 |
|
|
|a (NLM)24401145
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Ding, Bei
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Unveiling the membrane-binding properties of N-terminal and C-terminal regions of G protein-coupled receptor kinase 5 by combined optical spectroscopies
|
| 264 |
|
1 |
|c 2014
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 03.09.2014
|
| 500 |
|
|
|a Date Revised 06.05.2024
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a G protein-coupled receptor kinase 5 (GRK5) is thought to associate with membranes in part via N- and C-terminal segments that are typically disordered in available high-resolution crystal structures. Herein we investigate the interactions of these regions with model cell membrane using combined sum frequency generation (SFG) vibrational spectroscopy and attenuated total reflectance-Fourier transform infrared (ATR-FTIR) spectroscopy. It was found that both regions associate with POPC lipid bilayers but adopt different structures when doing so: GRK5 residues 2-31 (GRK5(2-31)) was in random coil whereas GRK5(546-565) was partially helical. When the subphase for the GRK5(2-31) peptide was changed to 40% TFE/60% 10 mM phosphate pH 7.4 buffer, a large change in the SFG amide I signal indicated that GRK5(2-31) became partially helical. By inspecting the membrane behavior of two different segments of GRK5(2-31), namely, GRK5(2-24) and GRK5(25-31), we found that residues 25-31 are responsible for membrane binding, whereas the helical character is imparted by residues 2-24. With SFG, we deduced that the orientation angle of the helical segment of GRK5(2-31) is 46 ± 1° relative to the surface normal in 40% TFE/60% 10 mM phosphate pH = 7.4 buffer but increases to 78 ± 11° with higher ionic strength. We also investigated the effect of PIP2 in the model membrane and concluded that the POPC:PIP2 (9:1) lipid bilayer did not change the behavior of either peptide compared to a pure POPC lipid bilayer. With ATR-FTIR, we also found that Ca(2+)·calmodulin is able to extract both peptides from the POPC lipid bilayer, consistent with the role of this protein in disrupting GRK5 interactions with the plasma membrane in cells
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, N.I.H., Extramural
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
7 |
|a Lipid Bilayers
|2 NLM
|
| 650 |
|
7 |
|a Phosphatidylcholines
|2 NLM
|
| 650 |
|
7 |
|a G-Protein-Coupled Receptor Kinase 5
|2 NLM
|
| 650 |
|
7 |
|a EC 2.7.11.16
|2 NLM
|
| 650 |
|
7 |
|a GRK5 protein, human
|2 NLM
|
| 650 |
|
7 |
|a EC 2.7.11.16
|2 NLM
|
| 650 |
|
7 |
|a 1-palmitoyl-2-oleoylphosphatidylcholine
|2 NLM
|
| 650 |
|
7 |
|a TE895536Y5
|2 NLM
|
| 700 |
1 |
|
|a Glukhova, Alisa
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Sobczyk-Kojiro, Katarzyna
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Mosberg, Henry I
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Tesmer, John J G
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Chen, Zhan
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 30(2014), 3 vom: 28. Jan., Seite 823-31
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
|
| 773 |
1 |
8 |
|g volume:30
|g year:2014
|g number:3
|g day:28
|g month:01
|g pages:823-31
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1021/la404055a
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_22
|
| 912 |
|
|
|a GBV_ILN_350
|
| 912 |
|
|
|a GBV_ILN_721
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 30
|j 2014
|e 3
|b 28
|c 01
|h 823-31
|