Biology:Golgi matrix
The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus.[1][2][3] The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent (which removed Golgi membranes) and 150 mM NaCl (which removed weakly associated proteins).[4] Treatment with a protease enzyme removed the matrix, which confirmed the importance of proteins for the matrix structure.[4] Modern freeze etch[5] electron microscopy (EM) clearly shows a mesh connecting Golgi cisternae and associated vesicles.[6][7] Further support for the existence of a matrix comes from EM images showing that ribosomes are excluded from regions between and near Golgi cisternae.[8][9][10][11][12][13]
Structure and function
The first individual protein component of the matrix was identified in 1995 as Golgin A2 (then called GM130).[14] Since then, many other golgin family proteins have been found to be in the Golgi matrix[2] and are associated with the Golgi membranes in a variety of ways.[15][1] For example, GMAP210 (Golgi Microtubule Associated Protein 210) has an ALPS (Amphipathic Lipid-Packing Sensor) motif in the N-termal 38 amino acids and an ARF1-binding domain called GRAB (Grip-Related Arf-Binding) at the C-terminus.[16] Thus, the GRAB-domain can bind indirectly to Golgi cisternae and its ALPS motif can tether vesicles.[17] Golgins have coiled-coil domains and are thus predicted to have elongated structures[2] up to 200 nm in length.[18] Most are peripheral membrane proteins attached at one end to Golgi membranes.[2] They have flexible regions between the coiled-coil domains, which make them ideal candidates for mediating the dynamic vesicle docking to Golgi cisternae and dynamic structure of the Golgi itself.[2]
Golgi reassembly-stacking proteins are an evolutionarily conserved family of proteins in the Golgi matrix.[2] GRASP65 and GRASP55 are the 2 human GRASPs. These proteins were named from their requirement for accurate Golgi reassembly during an in vitro assay,[2] but they have also been shown to function in vivo, as shown in the accompanying figure.[19] GRASPs associate with lipid bilayers because they are myristoylated and their myristic acid residue intercalates into the lipid layer.[7] Their trans oligomerization is controlled by phosphorylation[6] and is thought to explain the fragmentation of the Golgi as required during mitosis.[7]
Components
- Bicaudal D homolog
- CASP
- CG-NAP
- COH1
- GCC88
- GCC185
- GCP60
- Giantin
- GMAP210
- Golgin A2
- Golgin A7
- Golgin 45
- Golgin 67 and the product of duplicated gene GOLGA8A
- Golgin 84
- Golgin 97
- Golgin 160
- Golgin 245
- GORAB
- GRASP55
- GRASP65
- JAKMIP2
- JAKMIP3
- TMF1
- USO1
Disease associations
- CG-NAP hereditary Long QT syndrome LQT11[20]
- COH1 Cohen Syndrome[21]
- GMAP210 Achondrogenesis type IA[22]
- Golgin A2 a complex, neuromuscular disorder[23]
- GORAB Gerodermia osteodysplastica[24]
References
- ↑ 1.0 1.1 "Golgins and GTPases, giving identity and structure to the Golgi apparatus". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1744 (3): 383–95. 2005. doi:10.1016/j.bbamcr.2005.02.001. PMID 15979508.
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 "New components of the Golgi matrix". Cell and Tissue Research 344 (3): 365–79. 2011. doi:10.1007/s00441-011-1166-x. PMID 21494806.
- ↑ Lowe, M (2011). "Structural organization of the Golgi apparatus.". Current Opinion in Cell Biology 23 (1): 85–93. doi:10.1016/j.ceb.2010.10.004. PMID 21071196. https://zenodo.org/record/905674.
- ↑ 4.0 4.1 "Isolation of a matrix that binds medial Golgi enzymes". The Journal of Cell Biology 124 (4): 405–13. 1994. doi:10.1083/jcb.124.4.405. PMID 8106542.
- ↑ "The origins and evolution of freeze-etch electron microscopy". Journal of Electron Microscopy 60 (Suppl 1): S3–29. 2011. doi:10.1093/jmicro/dfr044. PMID 21844598.
- ↑ 6.0 6.1 Zhang, X. and Wang, Y. "Golgi structure and the role of GRASP65 in Golgi stack formation.". https://www.ncbi.nlm.nih.gov/core/lw/2.0/html/tileshop_pmc/tileshop_pmc_inline.html?title=Click%20on%20image%20to%20zoom&p=PMC3&id=4701983_fcell-03-00084-g0001.jpg.
- ↑ 7.0 7.1 7.2 Zhang, X. and Wang, Y., Front Cell Dev Biol. 2015; 3: 84. Published online 2016 Jan 6. doi: 10.3389/fcell.2015.00084 (2015). "GRASPs in Golgi Structure and Function". Frontiers in Cell and Developmental Biology 3: 84. doi:10.3389/fcell.2015.00084. PMID 26779480.
- ↑ Fig. 14 in "Tomographic Evidence for Continuous Turnover of Golgi Cisternae in Pichia pastoris". Molecular Biology of the Cell 14 (6): 2277–91. 2003. doi:10.1091/mbc.e02-10-0697. PMID 12808029.
- ↑ "Electron tomographic model of a Golgi stack and its encompassing, ribosome-excluding scaffold (Golgi matrix).". American Society of Plant Biologists. http://www.plantphysiol.org/content/147/4/1454/F5.expansion.html.
- ↑ "Transfer of COPII vesicles and their scaffolds to the cis-Golgi matrix". American Society of Plant Biologists. http://www.plantphysiol.org/content/147/4/1454/F4.large.jpg.
- ↑ "A mitotic form of the Golgi apparatus in HeLa cells". The Journal of Cell Biology 104 (4): 865–74. 1987. doi:10.1083/jcb.104.4.865. PMID 3104351.
- ↑ "Tomographic evidence for continuous turnover of Golgi cisternae in Pichia pastoris". Molecular Biology of the Cell 14 (6): 2277–91. 2003. doi:10.1091/mbc.E02-10-0697. PMID 12808029.
- ↑ "Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography". Plant Physiology 147 (4): 1454–68. 2008. doi:10.1104/pp.108.120618. PMID 18678738.
- ↑ "Characterization of a cis-Golgi matrix protein, GM130". The Journal of Cell Biology 131 (6 Pt 2): 1715–26. 1995. doi:10.1083/jcb.131.6.1715. PMID 8557739.
- ↑ Benjamin Short, Alexander Haas, Francis A. Barr. "Golgins associate with Golgi membranes in a variety of ways.". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. http://ars.els-cdn.com/content/image/1-s2.0-S016748890500011X-gr1.jpg.
- ↑ "Golgi localisation of GMAP210 requires two distinct cis-membrane binding mechanisms". BMC Biology 7: 56. 2009. doi:10.1186/1741-7007-7-56. PMID 19715559.
- ↑ "Membrane Curvature Sensing by Amphipathic Helices Is Modulated by the Surrounding Protein Backbone". PLOS ONE 10 (9): e0137965. 2015. doi:10.1371/journal.pone.0137965. PMID 26366573. Bibcode: 2015PLoSO..1037965D.
- ↑ "Asymmetric tethering of flat and curved lipid membranes by a golgin". Science 320 (5876): 670–3. 2008. doi:10.1126/science.1155821. PMID 18451304. Bibcode: 2008Sci...320..670D.
- ↑ "Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport". PLOS ONE 3 (2): e1647. 2008. doi:10.1371/journal.pone.0001647. PMID 18297130. Bibcode: 2008PLoSO...3.1647W.
- ↑ "Mutation of an A-kinase-anchoring protein causes long-QT syndrome". Proceedings of the National Academy of Sciences of the United States of America 104 (52): 20990–5. 2007. doi:10.1073/pnas.0710527105. PMID 18093912. Bibcode: 2007PNAS..10420990C.
- ↑ "Cohen syndrome is caused by mutations in a novel gene, COH1, encoding a transmembrane protein with a presumed role in vesicle-mediated sorting and intracellular protein transport". Am. J. Hum. Genet. 72 (6): 1359–69. 2003. doi:10.1086/375454. PMID 12730828.
- ↑ "Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210". The New England Journal of Medicine 362 (3): 206–16. 2010. doi:10.1056/NEJMoa0900158. PMID 20089971.
- ↑ "GOLGA2, encoding a master regulator of golgi apparatus, is mutated in a patient with a neuromuscular disorder". Human Genetics 135 (2): 245–51. 2016. doi:10.1007/s00439-015-1632-8. PMID 26742501.
- ↑ "Gerodermia osteodysplastica is caused by mutations in SCL1BP1, a Rab-6 interacting golgin". Nat. Genet. 40 (12): 1410–2. December 2008. doi:10.1038/ng.252. PMID 18997784.
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