CCR5 tyrosine sulfation heterogeneity generates cell surface receptor subpopulations with different ligand binding properties

Article Article scientifique Article CCR5 tyrosine sulfation heterogeneity generates cell surface receptor subpopulations with different ligand binding properties eng 2020 author Scurci Ilaria 847919 author Akondi Kalyana Bharati 882094 author De Magalhaes Pinheiro Inês 931460 author Paolini-Bertrand Marianne 663310 author Borgeat Alexia 799311 author Cerini Fabrice 23116 author Hartley Oliver 507767 129753 10.1016/j.bbagen.2020.129753 32991968 0304-4165 Chemokine receptor tyrosine sulfation plays a key role in the binding of chemokines. It has been suggested that receptor sulfation is heterogeneous, but no experimental evidence has been provided so far. The potent anti-HIV chemokine analog 5P12-RANTES has been proposed to owe its inhibitory activity to a capacity to bind a larger pool of cell surface CCR5 receptors than native chemokines such as CCL5, but the molecular details underlying this phenomenon have not been elucidated. Dewey 616.07 Swiss National Science Foundation Studying the modulation of CCR5 trafficking by chemokine analogues with potent anti-HIV activity 310030_163085 CH Project funding Swiss National Science Foundation Studying the modulation of CCR5 trafficking by chemokine analogues with potent anti-HIV activity 310030_184828 CH Project funding 137 Département de pathologie et immunologie 21F false 497 Hiv 835 Biochimica et Biophysica Acta - General Subjects 1865 1 fda517b0-83d5-46b5-bb15-adae1a4a2c6e Article (Published version) Public 1-s2.0-S0304416520302646-main.pdf 3629484 application/pdf CC BY 0f52da90-ca1a-42a7-8bd9-9ba3ed6cc408 Supplemental data Public 1-s2.0-S0304416520302646-mmc1.pdf 833912 application/pdf CC BY openAccess Faculté de médecine / Section de médecine fondamentale / Département de pathologie et immunologie

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CCR5 tyrosine sulfation heterogeneity generates cell surface receptor subpopulations with different ligand binding properties	Biochimica et Biophysica Acta - General Subjects			2020	218	154

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Borgeat, Alexia