Mechanisms of transport through the Golgi complex - PubMed (original) (raw)
Review
. 2009 Feb 15;122(Pt 4):443-52.
doi: 10.1242/jcs.032581.
Affiliations
- PMID: 19193869
- DOI: 10.1242/jcs.032581
Review
Mechanisms of transport through the Golgi complex
Catherine L Jackson. J Cell Sci. 2009.
Abstract
The Golgi complex is the central sorting and processing station of the secretory pathway, ensuring that cargo proteins, which are synthesized in the endoplasmic reticulum, are properly glycosylated and packaged into carriers for transport to their final destinations. Two recent studies highlight the fact that properties of membrane lipids play key roles in Golgi structural organization and trafficking. The Antonny laboratory has demonstrated the mechanism by which a Golgi tether containing a membrane-curvature-sensing domain at one end can link highly curved and flat membranes together in a reversible manner. In this way, a strong interaction that binds membranes together in an oriented fashion can easily be disrupted as the properties of the membranes change. The Lippincott-Schwartz laboratory has developed a new model for intra-Golgi trafficking, called the rapid-partitioning model, which incorporates lipid trafficking as an integral part. Simulations reveal that the sorting of lipids into processing and export domains that are connected to each Golgi cisterna, and bidirectional trafficking throughout the Golgi to allow proteins to associate with their preferred lipid environment, is sufficient to drive protein transport through the secretory pathway. Although only a proof in principle, this model for the first time invokes lipid sorting as the driving force in intra-Golgi trafficking, and provides a framework for future experimental work.
Similar articles
- New insights into membrane trafficking and protein sorting.
Derby MC, Gleeson PA. Derby MC, et al. Int Rev Cytol. 2007;261:47-116. doi: 10.1016/S0074-7696(07)61002-X. Int Rev Cytol. 2007. PMID: 17560280 Review. - Emerging new roles of the pre-Golgi intermediate compartment in biosynthetic-secretory trafficking.
Saraste J, Dale HA, Bazzocco S, Marie M. Saraste J, et al. FEBS Lett. 2009 Dec 3;583(23):3804-10. doi: 10.1016/j.febslet.2009.10.084. Epub 2009 Nov 1. FEBS Lett. 2009. PMID: 19887068 Review. - Live imaging of yeast Golgi cisternal maturation.
Matsuura-Tokita K, Takeuchi M, Ichihara A, Mikuriya K, Nakano A. Matsuura-Tokita K, et al. Nature. 2006 Jun 22;441(7096):1007-10. doi: 10.1038/nature04737. Epub 2006 May 14. Nature. 2006. PMID: 16699523 - The plant ER-Golgi interface: a highly structured and dynamic membrane complex.
Moreau P, Brandizzi F, Hanton S, Chatre L, Melser S, Hawes C, Satiat-Jeunemaitre B. Moreau P, et al. J Exp Bot. 2007;58(1):49-64. doi: 10.1093/jxb/erl135. Epub 2006 Sep 21. J Exp Bot. 2007. PMID: 16990376 Review. - Protein and lipid sorting from the trans-Golgi network to secretory granules-recent developments.
Thiele C, Huttner WB. Thiele C, et al. Semin Cell Dev Biol. 1998 Oct;9(5):511-6. doi: 10.1006/scdb.1998.0259. Semin Cell Dev Biol. 1998. PMID: 9835638 Review.
Cited by
- Searching for gold beyond mitosis: Mining intracellular membrane traffic in Aspergillus nidulans.
Peñalva MA, Galindo A, Abenza JF, Pinar M, Calcagno-Pizarelli AM, Arst HN, Pantazopoulou A. Peñalva MA, et al. Cell Logist. 2012 Jan 1;2(1):2-14. doi: 10.4161/cl.19304. Cell Logist. 2012. PMID: 22645705 Free PMC article. - Mechanisms of protein retention in the Golgi.
Banfield DK. Banfield DK. Cold Spring Harb Perspect Biol. 2011 Aug 1;3(8):a005264. doi: 10.1101/cshperspect.a005264. Cold Spring Harb Perspect Biol. 2011. PMID: 21525512 Free PMC article. Review. - Golgi phosphoprotein 3 triggers signal-mediated incorporation of glycosyltransferases into coatomer-coated (COPI) vesicles.
Eckert ES, Reckmann I, Hellwig A, Röhling S, El-Battari A, Wieland FT, Popoff V. Eckert ES, et al. J Biol Chem. 2014 Nov 7;289(45):31319-29. doi: 10.1074/jbc.M114.608182. Epub 2014 Sep 22. J Biol Chem. 2014. PMID: 25246532 Free PMC article. - Acylation - A New Means to Control Traffic Through the Golgi.
Ernst AM, Toomre D, Bogan JS. Ernst AM, et al. Front Cell Dev Biol. 2019 Jun 12;7:109. doi: 10.3389/fcell.2019.00109. eCollection 2019. Front Cell Dev Biol. 2019. PMID: 31245373 Free PMC article. Review. - Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions.
de Meyer FJ, Rodgers JM, Willems TF, Smit B. de Meyer FJ, et al. Biophys J. 2010 Dec 1;99(11):3629-38. doi: 10.1016/j.bpj.2010.09.030. Biophys J. 2010. PMID: 21112287 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources