Please use this identifier to cite or link to this item: http://repo.lib.jfn.ac.lk/ujrr/handle/123456789/192
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dc.contributor.authorAtcheson, E.
dc.contributor.authorHamilton, E
dc.contributor.authorPathmanathan, S
dc.contributor.authorGreer, B
dc.contributor.authorHarriott, P
dc.contributor.authorTimson, D.J
dc.date.accessioned2014-02-01T18:39:24Z
dc.date.accessioned2022-06-28T04:13:15Z-
dc.date.available2014-02-01T18:39:24Z
dc.date.available2022-06-28T04:13:15Z-
dc.date.issued2011-10
dc.identifier.issn01448463
dc.identifier.urihttp://repo.lib.jfn.ac.lk/ujrr/handle/123456789/192-
dc.description.abstractThe IQGAP [IQ-motif-containing GAP (GTPase-activating protein)] family members are eukaryotic proteins that act at the interface between cellular signalling and the cytoskeleton. As such they collect numerous inputs from a variety of signalling pathways. A key binding partner is the calcium-sensing protein CaM (calmodulin). This protein binds mainly through a series of IQ-motifs which are located towards the middle of the primary sequence of the IQGAPs. In some IQGAPs, these motifs also provide binding sites for CaM-like proteins such as myosin essential light chain and S100B. Using synthetic peptides and native gel electrophoresis, the binding properties of the IQ-motifs from human IQGAP2 and IQGAP3 have been mapped. The second and third IQ-motifs in IQGAP2 and all four of the IQ-motifs of IQGAP3 interacted with CaM in the presence of calcium ions. However, there were differences in the type of interaction: while some IQ-motifs were able to form complexes with CaM which were stable under the conditions of the experiment, others formed more transient interactions. The first IQ-motifs from IQGAP2 and IQGAP3 formed transient interactions with CaM in the absence of calcium and the first motif from IQGAP3 formed a transient interaction with the myosin essential light chain Mlc1sa. None of these IQ-motifs interacted with S100B. Molecular modelling suggested that all of the IQ-motifs, except the first one from IQGAP2 formed α-helices in solution. These results extend our knowledge of the selectivity of IQ-motifs for CaM and related proteins.en_US
dc.language.isoenen_US
dc.publisherBiochemical Societyen_US
dc.subjectα-helical peptideen_US
dc.subjectCalcium-dependent interactionen_US
dc.subjectIQ-motifen_US
dc.subjectIQ-motif-containing gtpase-activating protein (iqgap)en_US
dc.subjectMyosin essential light chainen_US
dc.subjectNative gel electrophoresisen_US
dc.titleIQ-motif selectivity in human IQGAP2 and IQGAP3: Binding of calmodulin and myosin essential light chainen_US
dc.typeArticleen_US
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