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Article: Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor

TitleFunctional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor
Authors
Issue Date2001
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2001, v. 142 n. 9, p. 3926-3934 How to Cite?
AbstractIn this study, a mutagenesis-based strategy was employed to assess the roles of two highly conserved motifs (KLR and RLAR) within the third endoloop of the human secretin receptor. Block deletion of KLRT and mutation of Lys323 (K323I) significantly reduced cAMP accumulation, and these mutations did not affect ligand interaction and receptor number expressed on the cell surface. Thus, the KLRT region at the N terminus of the third endoloop, particularly Lys323, is important for G protein coupling. For the RLAR motif, receptors with substitutions at positions 339 and 342 from Arg to Ala (R339, 342A), Glu (R339, 342E), or Ile (R339, 342I) as well as block deletion of the RLAR motif were all found to be defective in both secretin-binding and cAMP production. Interestingly, a single mutation at the corresponding positions of Arg339 or Arg342 responded as the wild-type human secretin receptor in all functional assays, indicating that the presence of one Arg at either position within the RLAR motif is sufficient for a normal receptor function. Immunofluorescent staining of these mutant receptors showed that these Arg residues are responsible for surface presentation and/or receptor stability.
Persistent Identifierhttp://hdl.handle.net/10722/84879
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, KYYen_HK
dc.contributor.authorPang, RTKen_HK
dc.contributor.authorChow, BKCen_HK
dc.date.accessioned2010-09-06T08:58:11Z-
dc.date.available2010-09-06T08:58:11Z-
dc.date.issued2001en_HK
dc.identifier.citationEndocrinology, 2001, v. 142 n. 9, p. 3926-3934en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84879-
dc.description.abstractIn this study, a mutagenesis-based strategy was employed to assess the roles of two highly conserved motifs (KLR and RLAR) within the third endoloop of the human secretin receptor. Block deletion of KLRT and mutation of Lys323 (K323I) significantly reduced cAMP accumulation, and these mutations did not affect ligand interaction and receptor number expressed on the cell surface. Thus, the KLRT region at the N terminus of the third endoloop, particularly Lys323, is important for G protein coupling. For the RLAR motif, receptors with substitutions at positions 339 and 342 from Arg to Ala (R339, 342A), Glu (R339, 342E), or Ile (R339, 342I) as well as block deletion of the RLAR motif were all found to be defective in both secretin-binding and cAMP production. Interestingly, a single mutation at the corresponding positions of Arg339 or Arg342 responded as the wild-type human secretin receptor in all functional assays, indicating that the presence of one Arg at either position within the RLAR motif is sufficient for a normal receptor function. Immunofluorescent staining of these mutant receptors showed that these Arg residues are responsible for surface presentation and/or receptor stability.en_HK
dc.languageengen_HK
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_HK
dc.relation.ispartofEndocrinologyen_HK
dc.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.titleFunctional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptoren_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=142&spage=3926&epage=3934&date=2001&atitle=Functional+Segregation+of+the+Highly+Conserved+Basic+Motifs+within+the+Third+Endoloop+of+the+Human+Secretin+Receptoren_HK
dc.identifier.emailPang, RTK: rtkpang@hku.hken_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityPang, RTK=rp01761en_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1210/en.142.9.3926en_HK
dc.identifier.pmid11517171-
dc.identifier.scopuseid_2-s2.0-0034864511en_HK
dc.identifier.hkuros65787en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034864511&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume142en_HK
dc.identifier.issue9en_HK
dc.identifier.spage3926en_HK
dc.identifier.epage3934en_HK
dc.identifier.isiWOS:000170689500025-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, KYY=25225022200en_HK
dc.identifier.scopusauthoridPang, RTK=7004376636en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK

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