scholarly journals Mapping the Membrane Topology and Extracellular Ligand Binding Domains of the Retinol Binding Protein Receptor†

Biochemistry ◽  
2008 ◽  
Vol 47 (19) ◽  
pp. 5387-5395 ◽  
Author(s):  
Riki Kawaguchi ◽  
Jiamei Yu ◽  
Patrick Wiita ◽  
Mariam Ter-Stepanian ◽  
Hui Sun
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Membrane Topology ◽  
Retinol Binding Protein ◽  
Binding Domains ◽  
Protein Receptor

scholarly journals Biochemical and NMR Mapping of the Interface between CREB-binding Protein and Ligand Binding Domains of Nuclear Receptor

2004 ◽  
Vol 280 (7) ◽  
pp. 5682-5692 ◽  
Author(s):  
Fabrice A. C. Klein ◽  
R. Andrew Atkinson ◽  
Noelle Potier ◽  
Dino Moras ◽  
Jean Cavarelli
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptor ◽  
Binding Protein ◽  
Creb Binding Protein ◽  
Binding Domains

scholarly journals Structural Studies of Retinol-Binding Protein Receptor RBPR2

2018 ◽  
Vol 114 (3) ◽  
pp. 424a
Author(s):  
Jonathan Kim ◽  
Yong Zi Tan ◽  
Brianna Costabile ◽  
Yunting Chen ◽  
Filippo Mancia
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Structural Studies ◽  
Protein Receptor

scholarly journals Solubilization and purification of the retinol-binding protein receptor from human placental membranes

1994 ◽  
Vol 302 (1) ◽  
pp. 245-251 ◽  
Author(s):  
A Sivaprasadarao ◽  
M Boudjelal ◽  
J B C Findlay
Keyword(s):  
Binding Protein ◽  
Binding Activity ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Sds Page ◽  
Minor Protein ◽  
Membrane Bound ◽  
Placental Membranes ◽  
Poly Ethylene ◽  
Solubilized Form

The membrane receptor for retinol-binding protein (RBP) has been solubilized from human placental brush-border membranes with octyl-beta-glucoside, Nonidet P-40 and CHAPS. A method, based on the preferential precipitation of 125I-RBP-receptor complex with poly(ethylene glycol) 8000, was developed in order to measure the RBP-binding activity in the detergent extracts. The receptor was fairly stable (4 degrees C, 7 days) in octyl-beta-glucoside and Nonidet P-40, but quickly lost activity in CHAPS. The detergent-solubilized form retained all the properties characteristic of the membrane-bound protein, except for a small decrease in affinity for RBP (3- and 7-fold in Nonidet P-40 and octyl-beta-glucoside respectively). The receptor was isolated using recombinant RBP coupled to Reacti-Gel 6X affinity matrix. The purified material contained major and minor protein species of 63 and 55 kDa respectively on SDS/PAGE.

scholarly journals Ligand Binding and Structural Analysis of a Human Putative Cellular Retinol-binding Protein

2002 ◽  
Vol 277 (44) ◽  
pp. 41970-41977 ◽  
Author(s):  
Claudia Folli ◽  
Vito Calderone ◽  
Ileana Ramazzina ◽  
Giuseppe Zanotti ◽  
Rodolfo Berni
Keyword(s):  
Structural Analysis ◽  
Ligand Binding ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Cellular Retinol Binding Protein

scholarly journals Galnt11 regulates kidney function by glycosylating the endocytosis receptor megalin to modulate ligand binding

2019 ◽  
Vol 116 (50) ◽  
pp. 25196-25202 ◽  
Author(s):  
E. Tian ◽  
Shengjun Wang ◽  
Liping Zhang ◽  
Ying Zhang ◽  
May C. Malicdan ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Kidney Function ◽  
Protein Function ◽  
Binding Protein ◽  
Association Studies ◽  
Retinol Binding Protein ◽  
Genome Wide Association Studies ◽  
Age Related ◽  
Deficient Mice

Chronic kidney disease (CKD) affects more than 20 million Americans and ∼10% of the population worldwide. Genome-wide association studies (GWAS) of kidney functional decline have identified genes associated with CKD, but the precise mechanisms by which they influence kidney function remained largely unexplored. Here, we examine the role of 1 GWAS-identified gene by creating mice deficient for Galnt11, which encodes a member of the enzyme family that initiates protein O-glycosylation, an essential posttranslational modification known to influence protein function and stability. We find that Galnt11-deficient mice display low-molecular-weight proteinuria and have specific defects in proximal tubule-mediated resorption of vitamin D binding protein, α1-microglobulin, and retinol binding protein. Moreover, we identify the endocytic receptor megalin (LRP2) as a direct target of Galnt11 in vivo. Megalin in Galnt11-deficient mice displays reduced ligand binding and undergoes age-related loss within the kidney. Differential mass spectrometry revealed specific sites of Galnt11-mediated glycosylation within mouse kidney megalin/LRP2 that are known to be involved in ligand binding, suggesting that O-glycosylation directly influences the ability to bind ligands. In support of this, recombinant megalin containing these sites displayed reduced albumin binding in cells deficient for Galnt11. Our results provide insight into the association between GALNT11 and CKD, and identify a role for Galnt11 in proper kidney function.

scholarly journals The retinol-binding protein receptor STRA6 regulates diurnal insulin responses

2017 ◽  
Vol 292 (36) ◽  
pp. 15080-15093 ◽  
Author(s):  
Christy M. Gliniak ◽  
J. Mark Brown ◽  
Noa Noy
Keyword(s):  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Insulin Responses

scholarly journals Cross Talk between Signaling and Vitamin A Transport by the Retinol-Binding Protein Receptor STRA6

2012 ◽  
Vol 32 (15) ◽  
pp. 3164-3175 ◽  
Author(s):  
D. C. Berry ◽  
S. M. O'Byrne ◽  
A. C. Vreeland ◽  
W. S. Blaner ◽  
N. Noy
Keyword(s):  
Vitamin A ◽  
Cross Talk ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor ◽  
Vitamin A Transport

scholarly journals Transthyretin Blocks Retinol Uptake and Cell Signaling by the Holo-Retinol-Binding Protein Receptor STRA6

2012 ◽  
Vol 32 (19) ◽  
pp. 3851-3859 ◽  
Author(s):  
D. C. Berry ◽  
C. M. Croniger ◽  
N. B. Ghyselinck ◽  
N. Noy
Keyword(s):  
Cell Signaling ◽  
Binding Protein ◽  
Retinol Binding Protein ◽  
Protein Receptor
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