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Article: Structure of the adaptor protein p14 reveals a profilin-like fold with distinct function

TitleStructure of the adaptor protein p14 reveals a profilin-like fold with distinct function
Authors
KeywordsMolecular Sequence Numbers
Issue Date2005
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal Of Molecular Biology, 2005, v. 347 n. 2, p. 309-321 How to Cite?
AbstractThe adaptor protein p14 is associated with the cytoplasmic face of late endosomes that is involved in cell-surface receptor endocytosis and it also directly interacts with MP1, a scaffolding protein that binds the MAP kinase ERK1 and its upstream kinase activator MEK1. The interaction of p14 with MP1 recruits the latter to late endosomes and the endosomal localization of p14/MP1-MEK1-ERK1 scaffolding complex is required for signaling via ERK MAP kinase in an efficient and specific manner upon receptor stimulation. Here, we report the three-dimensional solution structure of the adaptor protein p14. The structure reveals a profilin-like fold with a central five-stranded β-sheet sandwiched between α-helices. Unlike profilin, however, p14 exhibits weak interaction with selective phosphoinositides but no affinity towards proline-rich sequences. Structural comparison between profilin and p14 reveals the molecular basis for the differences in these functions. We further mapped the MP1 binding sites on p14 by NMR, and discuss the implications of these important findings on the possible function of p14. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91185
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorZhang, Qen_HK
dc.contributor.authorWang, Xen_HK
dc.contributor.authorZeng, Len_HK
dc.contributor.authorFarooq, Aen_HK
dc.contributor.authorZhou, MMen_HK
dc.date.accessioned2010-09-17T10:14:24Z-
dc.date.available2010-09-17T10:14:24Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Molecular Biology, 2005, v. 347 n. 2, p. 309-321en_HK
dc.identifier.issn0022-2836en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91185-
dc.description.abstractThe adaptor protein p14 is associated with the cytoplasmic face of late endosomes that is involved in cell-surface receptor endocytosis and it also directly interacts with MP1, a scaffolding protein that binds the MAP kinase ERK1 and its upstream kinase activator MEK1. The interaction of p14 with MP1 recruits the latter to late endosomes and the endosomal localization of p14/MP1-MEK1-ERK1 scaffolding complex is required for signaling via ERK MAP kinase in an efficient and specific manner upon receptor stimulation. Here, we report the three-dimensional solution structure of the adaptor protein p14. The structure reveals a profilin-like fold with a central five-stranded β-sheet sandwiched between α-helices. Unlike profilin, however, p14 exhibits weak interaction with selective phosphoinositides but no affinity towards proline-rich sequences. Structural comparison between profilin and p14 reveals the molecular basis for the differences in these functions. We further mapped the MP1 binding sites on p14 by NMR, and discuss the implications of these important findings on the possible function of p14. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_HK
dc.relation.ispartofJournal of Molecular Biologyen_HK
dc.subjectMolecular Sequence Numbersen_HK
dc.subject.meshAdaptor Proteins, Vesicular Transport - chemistry - genetics - metabolismen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshContractile Proteins - chemistryen_HK
dc.subject.meshEndosomes - chemistry - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMAP Kinase Signaling System - physiologyen_HK
dc.subject.meshMiceen_HK
dc.subject.meshMicrofilament Proteins - chemistryen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshPhospholipids - metabolismen_HK
dc.subject.meshPregnancy Proteinsen_HK
dc.subject.meshProfilinsen_HK
dc.subject.meshProline - metabolismen_HK
dc.subject.meshProtein Foldingen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshRecombinant Fusion Proteins - genetics - metabolismen_HK
dc.subject.meshSequence Alignmenten_HK
dc.titleStructure of the adaptor protein p14 reveals a profilin-like fold with distinct functionen_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2005.01.031en_HK
dc.identifier.pmid15740743-
dc.identifier.scopuseid_2-s2.0-14644420147en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-14644420147&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume347en_HK
dc.identifier.issue2en_HK
dc.identifier.spage309en_HK
dc.identifier.epage321en_HK
dc.identifier.isiWOS:000227565000007-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridZhang, Q=35546936300en_HK
dc.identifier.scopusauthoridWang, X=7501870078en_HK
dc.identifier.scopusauthoridZeng, L=7401904457en_HK
dc.identifier.scopusauthoridFarooq, A=7007061775en_HK
dc.identifier.scopusauthoridZhou, MM=7403506618en_HK

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