Please use this identifier to cite or link to this item: https://hdl.handle.net/1959.11/6198
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dc.contributor.authorKrishnan, Kannanen
dc.contributor.authorMoens, Pierreen
dc.date.accessioned2010-06-16T09:33:00Z-
dc.date.issued2009-
dc.identifier.citationBiophysical Reviews, 1(2), p. 71-81en
dc.identifier.issn1867-2469en
dc.identifier.issn1867-2450en
dc.identifier.urihttps://hdl.handle.net/1959.11/6198-
dc.description.abstractProfilins are small actin-binding proteins found in eukaryotes and certain viruses that are involved in cell development, cytokinesis, membrane trafficking, and cell motility. Originally identified as an actin sequestering/ binding protein, profilin has been involved in actin polymerization dynamics. It catalyzes the exchange of ADP/ATP in actin and increases the rate of polymerization. Profilins also interact with polyphosphoinositides (PPI) and proline-rich domains containing proteins. Through its interaction with PPIs, profilin has been linked to signaling pathways between the cell membrane and the cytoskeleton, while its role in membrane trafficking has been associated with its interaction with proline-rich domain-containing proteins. Depending on the organism, profilin is present in a various number of isoforms. Four isoforms of profilin have been reported in higher organisms, while only one or two isoforms are expressed in single-cell organisms. The affinity of these isoforms for their ligands varies between isoforms and should therefore modulate their functions. However, the significance and the functions of the different isoforms are not yet fully understood. The structures of many profilin isoforms have been solved both in the presence and the absence of actin and poly-L-proline. These structural studies will greatly improve our understanding of the differences and similarities between the different profilins. Structural stability studies of different profilins are also shedding some light on our understanding of the profilin/ligand interactions. Profilin is a multifaceted protein for which a dramatic increase in potential functions has been found in recent years; as such, it has been implicated in a variety of physiological and pathological processes.en
dc.languageenen
dc.publisherSpringeren
dc.relation.ispartofBiophysical Reviewsen
dc.titleStructure and functions of profilinsen
dc.typeJournal Articleen
dc.identifier.doi10.1007/s12551-009-0010-yen
dc.subject.keywordsProteomics and Intermolecular Interactions (excl Medical Proteomics)en
dc.subject.keywordsStructural Biology (incl Macromolecular Modelling)en
dc.subject.keywordsBiological Physicsen
local.contributor.firstnameKannanen
local.contributor.firstnamePierreen
local.subject.for2008060109 Proteomics and Intermolecular Interactions (excl Medical Proteomics)en
local.subject.for2008060112 Structural Biology (incl Macromolecular Modelling)en
local.subject.for2008029901 Biological Physicsen
local.subject.seo2008970106 Expanding Knowledge in the Biological Sciencesen
local.profile.schoolHuman Biology and Physiologyen
local.profile.schoolSchool of Science and Technologyen
local.profile.emailkkrishna@une.edu.auen
local.profile.emailpmoens@une.edu.auen
local.output.categoryC1en
local.record.placeauen
local.record.institutionUniversity of New Englanden
local.identifier.epublicationsrecordune-20090629-120931en
local.publisher.placeGermanyen
local.format.startpage71en
local.format.endpage81en
local.identifier.scopusid82155202494en
local.identifier.volume1en
local.identifier.issue2en
local.contributor.lastnameKrishnanen
local.contributor.lastnameMoensen
dc.identifier.staffune-id:kkrishnaen
dc.identifier.staffune-id:pmoensen
local.profile.orcid0000-0003-3121-5306en
local.profile.roleauthoren
local.profile.roleauthoren
local.identifier.unepublicationidune:6355en
dc.identifier.academiclevelAcademicen
dc.identifier.academiclevelAcademicen
local.title.maintitleStructure and functions of profilinsen
local.output.categorydescriptionC1 Refereed Article in a Scholarly Journalen
local.search.authorKrishnan, Kannanen
local.search.authorMoens, Pierreen
local.open.fileurlhttps://rune.une.edu.au/web/retrieve/b44fee71-3147-49ff-b6a2-5781f7c8bcc2en
local.uneassociationUnknownen
local.year.published2009en
local.fileurl.openhttps://rune.une.edu.au/web/retrieve/b44fee71-3147-49ff-b6a2-5781f7c8bcc2en
Appears in Collections:Journal Article
School of Science and Technology
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