How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifs

Handle URI:
http://hdl.handle.net/10754/565983
Title:
How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifs
Authors:
Alam, Tanvir ( 0000-0003-4844-0171 ) ; Alazmi, Meshari; Gao, Xin ( 0000-0002-7108-3574 ) ; Arold, Stefan T. ( 0000-0001-5278-0668 )
Abstract:
LD motifs (leucine-aspartic acidmotifs) are short helical protein-protein interaction motifs that have emerged as key players in connecting cell adhesion with cell motility and survival. LD motifs are required for embryogenesis, wound healing and the evolution of multicellularity. LD motifs also play roles in disease, such as in cancer metastasis or viral infection. First described in the paxillin family of scaffolding proteins, LD motifs and similar acidic LXXLL interaction motifs have been discovered in several other proteins, whereas 16 proteins have been reported to contain LDBDs (LD motif-binding domains). Collectively, structural and functional analyses have revealed a surprising multivalency in LD motif interactions and a wide diversity in LDBD architectures. In the present review, we summarize the molecular basis for function, regulation and selectivity of LD motif interactions that has emerged from more than a decade of research. This overview highlights the intricate multi-level regulation and the inherently noisy and heterogeneous nature of signalling through short protein-protein interaction motifs. © 2014 Biochemical Society.
KAUST Department:
Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division; Biological and Environmental Sciences and Engineering (BESE) Division
Publisher:
Portland Press Ltd.
Journal:
Biochemical Journal
Issue Date:
29-May-2014
DOI:
10.1042/BJ20140298
PubMed ID:
24870021
Type:
Article
ISSN:
02646021
Sponsors:
This work was supported by funding from the King Abdullah University of Science and Technology (KAUST). T.A. was supported by a KAUST Baseline fund to Vladimir B. Bajic.
Appears in Collections:
Articles; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division; Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorAlam, Tanviren
dc.contributor.authorAlazmi, Mesharien
dc.contributor.authorGao, Xinen
dc.contributor.authorArold, Stefan T.en
dc.date.accessioned2015-08-12T08:58:05Zen
dc.date.available2015-08-12T08:58:05Zen
dc.date.issued2014-05-29en
dc.identifier.issn02646021en
dc.identifier.pmid24870021en
dc.identifier.doi10.1042/BJ20140298en
dc.identifier.urihttp://hdl.handle.net/10754/565983en
dc.description.abstractLD motifs (leucine-aspartic acidmotifs) are short helical protein-protein interaction motifs that have emerged as key players in connecting cell adhesion with cell motility and survival. LD motifs are required for embryogenesis, wound healing and the evolution of multicellularity. LD motifs also play roles in disease, such as in cancer metastasis or viral infection. First described in the paxillin family of scaffolding proteins, LD motifs and similar acidic LXXLL interaction motifs have been discovered in several other proteins, whereas 16 proteins have been reported to contain LDBDs (LD motif-binding domains). Collectively, structural and functional analyses have revealed a surprising multivalency in LD motif interactions and a wide diversity in LDBD architectures. In the present review, we summarize the molecular basis for function, regulation and selectivity of LD motif interactions that has emerged from more than a decade of research. This overview highlights the intricate multi-level regulation and the inherently noisy and heterogeneous nature of signalling through short protein-protein interaction motifs. © 2014 Biochemical Society.en
dc.description.sponsorshipThis work was supported by funding from the King Abdullah University of Science and Technology (KAUST). T.A. was supported by a KAUST Baseline fund to Vladimir B. Bajic.en
dc.publisherPortland Press Ltd.en
dc.subjectCanceren
dc.subjectNuclear export signalen
dc.subjectNuclear receptoren
dc.subjectProtein-ligand interactionen
dc.subjectSignallingen
dc.subjectVirus-host interactionen
dc.titleHow to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifsen
dc.typeArticleen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentComputer, Electrical and Mathematical Sciences and Engineering (CEMSE) Divisionen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalBiochemical Journalen
kaust.authorAlam, Tanviren
kaust.authorGao, Xinen
kaust.authorArold, Stefan T.en
kaust.authorAlazmi, Mesharien

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