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The G protein coupled receptor CXCR4 designed by the QTY code becomes more hydrophilic and retains cell signaling activity.

ABSTRACT: G protein-coupled receptors (GPCRs) are vital for diverse biological functions, including vision, smell, and aging. They are involved in a wide range of diseases, and are among the most important targets of medicinal drugs. Tools that facilitate GPCR studies or GPCR-based technologies or therapies are thus critical to develop. Here we report using our QTY (glutamine, threonine, tyrosine) code to systematically replace 29 membrane-facing leucine, isoleucine, valine, and phenylalanine residues in the transmembrane ?-helices of the GPCR CXCR4. This variant, CXCR4^QTY29, became more hydrophilic, while retaining the ability to bind its ligand CXCL12. When transfected into HEK293 cells, it inserted into the cell membrane, and initiated cellular signaling. This QTY code has the potential to improve GPCR and membrane protein studies by making it possible to design functional hydrophilic receptors. This tool can be applied to diverse ?-helical membrane proteins, and may aid in the development of other applications, including clinical therapies.

SUBMITTER: Tegler L

PROVIDER: S-EPMC7721705 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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The G protein coupled receptor CXCR4 designed by the QTY code becomes more hydrophilic and retains cell signaling activity.

Tegler Lotta L Corin Karolina K Pick Horst H Brookes Jennifer J Skuhersky Michael M Vogel Horst H Zhang Shuguang S

Scientific reports 20201207 1

G protein-coupled receptors (GPCRs) are vital for diverse biological functions, including vision, smell, and aging. They are involved in a wide range of diseases, and are among the most important targets of medicinal drugs. Tools that facilitate GPCR studies or GPCR-based technologies or therapies are thus critical to develop. Here we report using our QTY (glutamine, threonine, tyrosine) code to systematically replace 29 membrane-facing leucine, isoleucine, valine, and phenylalanine residues in ...[more]

PMID: 33288780

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Project description:The retention of participants in studies is important for the validity of research. We updated our prior systematic review (2005) to assess retention strategies for in-person follow-up in health care studies.We searched PubMed, Cumulative Index of Nursing and Allied Health Literature, Cochrane Controlled Trials Register, Cochrane Methodology Register, and Embase (August 2013) for English-language reports of studies that described retention strategies for in-person follow-up in health care studies. We abstracted each retention strategy, and two authors independently classified each retention strategy with one of the themes developed in our prior review.We identified 88 studies (67 newly identified studies), six of which were designed to compare retention strategies, whereas the remainder described retention strategies and retention rates. There were 985 strategies abstracted from the descriptive studies (617 from new studies), with a median (interquartile range) number of strategies per study of 10 (7 to 17) and a median (interquartile range) number of themes per study of 6 (4 to 7). Financial incentives were used in 47 (57%) of the descriptive studies. We classified 28% of the strategies under the theme of "contact and scheduling methods," with 83% of the identified studies using at least one strategy within this theme. The number of strategies used was positively correlated with retention rate (P = 0.027), but the number of themes was not associated with retention rate (P = 0.469).The number of studies describing retention strategies has substantially increased since our prior review. However, the lack of comparative studies and the heterogeneity in the types of strategies, participant population and study designs, prohibits synthesis to determine the types of cohort retention strategies that were most effective. However, using a larger number of retention strategies, across five or six different themes, appears to retain more study participants.

Dataset Information

The G protein coupled receptor CXCR4 designed by the QTY code becomes more hydrophilic and retains cell signaling activity.

Publications

The G protein coupled receptor CXCR4 designed by the QTY code becomes more hydrophilic and retains cell signaling activity.

Similar Datasets

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