Assembly and disassembly of the Golgi complex: two processes arranged in a cis-trans direction
- PMID: 1730750
- PMCID: PMC2289264
- DOI: 10.1083/jcb.116.1.69
Assembly and disassembly of the Golgi complex: two processes arranged in a cis-trans direction
Abstract
We have studied the disassembly and assembly of two morphologically and functionally distinct parts of the Golgi complex, the cis/middle and trans cisterna/trans network compartments. For this purpose we have followed the redistribution of three cis/middle- (GMPc-1, GMPc-2, MG 160) and two trans- (GMPt-1 and GMPt-2) Golgi membrane proteins during and after treatment of normal rat kidney (NRK) cells with brefeldin A (BFA). BFA induced complete disassembly of the cis/middle- and trans-Golgi complex and translocation of GMPc and GMPt to the ER. Cells treated for short times (3 min) with BFA showed extensive disorganization of both cis/middle- and trans-Golgi complexes. However, complete disorganization of the trans part required much longer incubations with the drug. Upon removal of BFA the Golgi complex was reassembled by a process consisting of three steps: (a) exist of cis/middle proteins from the ER and their accumulation into vesicular structures scattered throughout the cytoplasm; (b) gradual relocation and accumulation of the trans proteins in the vesicles containing the cis/middle proteins; and (c) assembly of the cisternae, and reconstruction of the Golgi complex within an area located in the vicinity of the centrosome from which the ER was excluded. Reconstruction of the cis/middle-Golgi complex occurred under temperature conditions inhibitory of the reorganization of the trans-Golgi complex, and was dependent on microtubules. Reconstruction of the trans-Golgi complex, disrupted with nocodazole after selective fusion of the cis/middle-Golgi complex with the ER, occurred after the release of cis/middle-Golgi proteins from the ER and the assembly of the cis/middle cisternae.
Similar articles
-
Effects of brefeldin A on the three-dimensional structure of the Golgi apparatus in a sensitive strain of Saccharomyces cerevisiae.Anat Rec. 1995 Jan;241(1):1-9. doi: 10.1002/ar.1092410102. Anat Rec. 1995. PMID: 7879913
-
Presence of Golgi remnant membranes in the cytoplasm of brefeldin A-treated cells.Eur J Cell Biol. 1992 Aug;58(2):214-27. Eur J Cell Biol. 1992. PMID: 1425763
-
A Golgi-related structure remains after the brefeldin A-induced formation of an ER-Golgi hybrid compartment.Eur J Cell Biol. 1992 Aug;58(2):187-201. Eur J Cell Biol. 1992. PMID: 1425761
-
Microtubules and the organization of the Golgi complex.Exp Cell Res. 1985 Jul;159(1):1-16. doi: 10.1016/s0014-4827(85)80032-x. Exp Cell Res. 1985. PMID: 3896822 Review.
-
Dynamics of the interphase mammalian Golgi complex as revealed through drugs producing reversible Golgi disassembly.Biochim Biophys Acta. 1998 Aug 14;1404(1-2):127-37. doi: 10.1016/s0167-4889(98)00053-6. Biochim Biophys Acta. 1998. PMID: 9714774 Review.
Cited by
-
PDMP blocks brefeldin A-induced retrograde membrane transport from golgi to ER: evidence for involvement of calcium homeostasis and dissociation from sphingolipid metabolism.J Cell Biol. 1998 Jul 13;142(1):25-38. doi: 10.1083/jcb.142.1.25. J Cell Biol. 1998. PMID: 9660860 Free PMC article.
-
Sequential depletion and acquisition of proteins during Golgi stack disassembly and reformation.Traffic. 2010 Nov;11(11):1429-44. doi: 10.1111/j.1600-0854.2010.01106.x. Epub 2010 Aug 18. Traffic. 2010. PMID: 20716110 Free PMC article.
-
Ordered assembly of the duplicating Golgi in Trypanosoma brucei.Proc Natl Acad Sci U S A. 2006 May 16;103(20):7676-81. doi: 10.1073/pnas.0602595103. Epub 2006 May 3. Proc Natl Acad Sci U S A. 2006. PMID: 16672362 Free PMC article.
-
Alternative fates of newly formed PrPSc upon prion conversion on the plasma membrane.J Cell Sci. 2013 Aug 15;126(Pt 16):3552-62. doi: 10.1242/jcs.120477. Epub 2013 Jun 26. J Cell Sci. 2013. PMID: 23813960 Free PMC article.
-
Poliovirus infection and expression of the poliovirus protein 2B provoke the disassembly of the Golgi complex, the organelle target for the antipoliovirus drug Ro-090179.J Virol. 1997 Jun;71(6):4679-93. doi: 10.1128/JVI.71.6.4679-4693.1997. J Virol. 1997. PMID: 9151862 Free PMC article.