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dc.contributor.authorCobbold, C
dc.contributor.authorCoventry, J
dc.contributor.authorPonnambalam, S
dc.contributor.authorMonaco, AP
dc.date.accessioned2017-05-03T15:03:55Z
dc.date.available2017-05-03T15:03:55Z
dc.date.issued2004
dc.date.modified2009-12-21T06:46:38Z
dc.identifier.issn0968-7688
dc.identifier.doi10.1080/096870310001607350
dc.identifier.urihttp://hdl.handle.net/10072/27877
dc.description.abstractThe Menkes disease ATPase (MNK) is a copper transporter that localizes to the mammalian trans-Golgi network (TGN) and shows substantial co-localization with a ubiquitous TGN resident protein and marker, TGN46. We tested our hypothesis that these two TGN residents and integral membrane proteins are localized to biochemically distinct TGN sub-compartments using constitutively active mutant proteins and drugs that disrupt membrane traffic, lumenal pH and the cellular cytoskeleton. The pH-disrupting agent, monensin, causes MNK to be more diffusely distributed with partial separation of staining patterns for these two TGN residents. Expression of a constitutively active Rho-kinase (ROCK-KIN), which causes formation of juxta-nuclear astral actin arrays, also effects separation of MNK and TGN46 staining patterns. Treatment of ROCK-KIN expressing cells with latrunculin B, an actin-depolymerizing agent, causes complete overlap of MNK and TGN46 staining patterns with concomitant disappearance of polymerized actin. When microtubules are depolymerized in ROCK-KIN expressing cells by nocodazole, both MNK and TGN46 are found in puncate structures throughout the cell. However, a substantial proportion of MNK is still found in a juxta-nuclear location in contrast to TGN46. Actin distribution in these cells reveals that juxtanuclear MNK is distinct to the astral actin clusters in ROCK-KIN expressing cells where the microtubules were depolymerized. The TGN to cell-surface transport of MNK requires both actin and microtubule networks, whilst the constitutive trafficking of proteins is independent of actin. Taken together, our findings indicate that at least two TGN sub-domains are regulated by separate cytoskeletal dynamics involving actin and tubulin.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherTaylor and Francis
dc.publisher.placeUK
dc.publisher.urihttp://www.informaworld.com/smpp/title~content=t713693962~db=all
dc.relation.ispartofpagefrom59
dc.relation.ispartofpageto66
dc.relation.ispartofissue1
dc.relation.ispartofjournalMolecular Membrane Biology
dc.relation.ispartofvolume21
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode0601
dc.titleActin and microtubule regulation of trans-Golgi network architecture, and copper-dependent protein transport to the cell surface
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2004
gro.hasfulltextNo Full Text
gro.griffith.authorCobbold, Christian J.


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