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dc.contributor.authorMunn, Alan L
dc.contributor.authorThanabalu, Thirumaran
dc.date.accessioned2017-05-03T15:29:16Z
dc.date.available2017-05-03T15:29:16Z
dc.date.issued2009
dc.date.modified2010-08-19T07:05:10Z
dc.identifier.issn1521-6543
dc.identifier.doi10.1002/iub.195
dc.identifier.urihttp://hdl.handle.net/10072/30097
dc.description.abstractSpatiotemporal organisation of eukaryotic cells is established and maintained by the cytoskeleton, a highly dynamic and complex network of structural and signalling proteins. Many components of the cytoskeleton are functionally and structurally conserved between humans and yeast. Among these are verprolin (Vrp1p) in yeast and its human ortholog Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP). Much of our understanding of the function of these proteins has come from genetic analysis in yeast. Verprolin-deficient yeast cells exhibit defects in cytokinesis, endocytosis, and actin cytoskeleton polarisation. Verprolin binds actin, the yeast ortholog of human WASP (Las17p or Bee1p), and the yeast ortholog of human PSTPIP1 (Hof1p or Cyk2p). We propose that verprolin acts as a chaperone that by transient bimolecular interactions maintains the proper function of its partners. Verprolin-related proteins and partners are implicated in cancer, immunodeficiency, and neurodegeneration. Therefore, elucidating how verprolin functions will have major impacts in cell biology and medicine.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent267670 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherWiley-Blackwell Publishing Ltd.
dc.publisher.placeUnited Kingdom
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom707
dc.relation.ispartofpageto712
dc.relation.ispartofissue7
dc.relation.ispartofjournalIUBMB Life
dc.relation.ispartofvolume61
dc.rights.retentionN
dc.subject.fieldofresearchBiochemistry and cell biology
dc.subject.fieldofresearchGenetics
dc.subject.fieldofresearchMedical biochemistry and metabolomics
dc.subject.fieldofresearchcode3101
dc.subject.fieldofresearchcode3105
dc.subject.fieldofresearchcode3205
dc.titleVerprolin: A cool set of actin-binding sites and some very HOT prolines
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.facultyGriffith Health, School of Medical Science
gro.rights.copyright© 2009 International Union of Biochemistry and Molecular Biology, Inc. Published by Wiley-Blackwell Publishing. This is the author-manuscript version of the paper. Reproduced in accordance with the copyright policy of the publisher. The definitive version is available at www.interscience.wiley.com
gro.date.issued2009
gro.hasfulltextFull Text
gro.griffith.authorMunn, Alan L.


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