Substitution of the cysteine 438 residue in the cytoplasmic tail of the glucagon-like peptide-1 receptor alters signal transduction activity

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dc.contributor.authorVázquez Pérez, Patricia
dc.contributor.authorRoncero Rincón, Isabel
dc.contributor.authorBlázquez Fernández, Enrique
dc.contributor.authorÁlvarez García, Elvira
dc.contributor.editorBioscientifica
dc.date.accessioned2024-01-29T15:41:09Z
dc.date.available2024-01-29T15:41:09Z
dc.date.issued2005
dc.description.abstractSeveral G-protein-coupled receptors contain cysteine residues in the C-terminal tail that may modulate receptor function. In this work we analysed the substitution of Cys438 by alanine in the glucagon-like peptide-1 (GLP-1) receptor (GLPR), which led to a threefold decrease in cAMP production, although endocytosis and cellular redistribution of GLP-1 receptor agonist-induced processes were unaffected. Additionally, cysteine residues in the C-terminal tail of several G-protein-coupled receptors were found to act as substrates for palmitoylation, which might modify the access of protein kinases to this region. His-tagged GLP-1 receptors incorporated 3H-palmitate. Nevertheless, substitution of Cys438 prevented the incorporation of palmitate. Accordingly, we also investigated the effect of substitution of the consensus sequence by protein kinase C (PKC) Ser431/432 in both wild-type and Ala438 GLP-1 receptors. Substitution of Ser431/432 by alanine did not modify the ability of wild-type receptors to stimulate adenylate cyclase or endocytosis and recycling processes. By contrast, the substitution of Ser431/432 by alanine in the receptor containing Ala438 increased the ability to stimulate adenylate cyclase. All types of receptors were mainly internalised through coated pits. Thus, cysteine 438 in the cytoplasmic tail of the GLP-1 receptor would regulate its interaction with G-proteins and the stimulation of adenylyl cyclase. Palmitoylation of this residue might control the access of PKC to Ser431/432.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Medicina
dc.description.refereedTRUE
dc.description.statuspub
dc.identifier.citationVázquez P, Roncero I, Blázquez E, Alvarez E. Substitution of the cysteine 438 residue in the cytoplasmic tail of the glucagon-like peptide-1 receptor alters signal transduction activity. J Endocrinol. 2005;185(1):35-44. doi:10.1677/joe.1.06031
dc.identifier.doi10.1677/joe.1.06031
dc.identifier.issn0022-0795
dc.identifier.issn1479-6805
dc.identifier.officialurlhttps://doi.org/10.1677/joe.1.06031
dc.identifier.urihttps://hdl.handle.net/20.500.14352/96187
dc.issue.number1
dc.journal.titleJournal of Endocrinology
dc.language.isoeng
dc.page.final44
dc.page.initial35
dc.publisherBioScientifica
dc.rightsAttribution 4.0 Internationalen
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subject.cdu612.017
dc.subject.ucmCiencias Biomédicas
dc.subject.unesco24 Ciencias de la Vida
dc.titleSubstitution of the cysteine 438 residue in the cytoplasmic tail of the glucagon-like peptide-1 receptor alters signal transduction activity
dc.typejournal article
dc.type.hasVersionVoR
dc.volume.number185
dspace.entity.typePublication
relation.isAuthorOfPublication10be4d39-6db9-4c8f-ab13-81da235fb32f
relation.isAuthorOfPublicationfb1cab9c-180a-467f-817f-67fb1aaa7364
relation.isAuthorOfPublication14257552-0618-4a80-a697-15d4084de45d
relation.isAuthorOfPublication.latestForDiscovery10be4d39-6db9-4c8f-ab13-81da235fb32f
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