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The Flightless I protein and the gelsolin family in nuclear hormone receptor-mediated signalling

Archer, Stuart; Behm, Carolyn; Claudianos, Charles; Campbell, Hugh

Description

The Drosophila melanogaster flightless I protein and its homologues in higher eukaryotes (Flil) are conserved members of the gelsolin family of actin-binding proteins. Members of the gelsolin family generally contain three or six copies of a 125-amino-acid residue gelsolin-related repeating unit, and may contain additional domains including the C-terminal villin-related 'headpiece' or N-terminal extensions such as the leucine-rich repeat of the Flil protein. Numerous studies including work done...[Show more]

dc.contributor.authorArcher, Stuart
dc.contributor.authorBehm, Carolyn
dc.contributor.authorClaudianos, Charles
dc.contributor.authorCampbell, Hugh
dc.date.accessioned2015-12-13T23:07:37Z
dc.date.available2015-12-13T23:07:37Z
dc.identifier.issn0300-5127
dc.identifier.urihttp://hdl.handle.net/1885/86286
dc.description.abstractThe Drosophila melanogaster flightless I protein and its homologues in higher eukaryotes (Flil) are conserved members of the gelsolin family of actin-binding proteins. Members of the gelsolin family generally contain three or six copies of a 125-amino-acid residue gelsolin-related repeating unit, and may contain additional domains including the C-terminal villin-related 'headpiece' or N-terminal extensions such as the leucine-rich repeat of the Flil protein. Numerous studies including work done with mouse knockouts for gelsolin, villin and CapG support a role for the family in cytoskeletal actin dynamics. In both fruitfly and mouse, the Flil protein is also essential for early development. Recent studies indicate that supervillin, gelsolin and Flil are involved in intracellular signalling via nuclear hormone receptors including the androgen, oestrogen and thyroid hormone receptors. This unexpected role in signalling has opened a new area in research on the gelsolin family and is providing important new insights into the mechanisms of gene regulation via nuclear receptors.
dc.publisherPortland Press
dc.sourceBiochemical Society Transactions
dc.subjectKeywords: actin; actin binding protein; amino acid; androgen receptor; CapG protein; cell nucleus receptor; estrogen receptor; Flightless I protein; flil protein; gelsolin; hormone receptor; leucine; protein; supervillin; thyroid hormone receptor; unclassified drug Androgen receptor; Flightless I; Gelsolin; Nuclear hormone receptor; Oestrogen receptor; Supervillin
dc.titleThe Flightless I protein and the gelsolin family in nuclear hormone receptor-mediated signalling
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume32
dc.date.issued2004
local.identifier.absfor060405 - Gene Expression (incl. Microarray and other genome-wide approaches)
local.identifier.ariespublicationMigratedxPub15112
local.type.statusPublished Version
local.contributor.affiliationArcher, Stuart, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationBehm, Carolyn, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationClaudianos, Charles, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationCampbell, Hugh, College of Medicine, Biology and Environment, ANU
local.bibliographicCitation.issue6
local.bibliographicCitation.startpage940
local.bibliographicCitation.lastpage942
local.identifier.doi10.1042/BST0320940
dc.date.updated2015-12-12T08:09:58Z
local.identifier.scopusID2-s2.0-10644295590
CollectionsANU Research Publications

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