Actin and microtubule regulation of Trans-Golgi network architecture, and copper-dependent protein transport to the cell surface

Cobbold, Christian, Coventry, Julie, Ponnambalam, Sreenivasan and Monaco, Anthony P. (2004) Actin and microtubule regulation of Trans-Golgi network architecture, and copper-dependent protein transport to the cell surface. Molecular Membrane Biology, 21 1: 59-66.


Author Cobbold, Christian
Coventry, Julie
Ponnambalam, Sreenivasan
Monaco, Anthony P.
Title Actin and microtubule regulation of Trans-Golgi network architecture, and copper-dependent protein transport to the cell surface
Journal name Molecular Membrane Biology   Check publisher's open access policy
ISSN 1464-5203
0968-7688
Publication date 2004-01
Year available 2004
Sub-type Article (original research)
DOI 10.1080/096870310001607350
Volume 21
Issue 1
Start page 59
End page 66
Total pages 8
Place of publication London
Publisher Informa Healthcare
Language eng
Subject 06 Biological Sciences
0601 Biochemistry and Cell Biology
11 Medical and Health Sciences
1101 Medical Biochemistry and Metabolomics
Abstract The 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 juxta-nuclear 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.
Keyword Trans-Golgi network (TGN)
Rhoinase (ROCK)
Actin
Microtubules
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Biomedical Sciences Publications
 
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