Traffic between the plant endoplasmic reticulum and Golgi apparatus: to the Golgi and beyond

Current Opinion in Plant Biology

Volumn 9, Issue 6, 2006, Pages 601-609

  Matheson, Loren A ^a   Hanton, Sally L ^a   Brandizzi, Federica ^a,b  

^a UNIVERSITY OF SASKATCHEWAN   (Canada)

^b MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; METABOLISM; PLANT; PROTEIN TRANSPORT; REVIEW;

ENDOPLASMIC RETICULUM; GOLGI APPARATUS; PLANTS; PROTEIN TRANSPORT;

EID: 33749563351     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2006.09.016     Document Type: Review

References (52)

1. Hanton S.L., Matheson L.A., and Brandizzi F. Seeking a way out: export of proteins from the plant endoplasmic reticulum. Trends Plant Sci 11 (2006) 335-343
2. daSilva L.L., Snapp E.L., Denecke J., Lippincott-Schwartz J., Hawes C., and Brandizzi F. Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 16 (2004) 1753-1771
3. Yang Y.D., Elamawi R., Bubeck J., Pepperkok R., Ritzenthaler C., and Robinson D.G. Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites. Plant Cell 17 (2005) 1513-1531
4. Stefano G., Renna L., Chatre L., Hanton S.L., Moreau P., Hawes C., and Brandizzi F. In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery. Plant J 46 (2006) 95-110
5. Hanton S.L., Renna L., Bortolotti L.E., Chatre L., Stefano G., and Brandizzi F. Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells. Plant Cell 17 (2005) 3081-3093. Diacidic motifs are shown to perform a significant function in the export of multispanning, type II and type I membrane proteins to the Golgi apparatus. The findings described in this paper indicate that diacidic ER export motifs are dominant over transmembrane domain length in determining the export of proteins from the ER.
6. Contreras I., Yang Y., Robinson D.G., and Aniento F. Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat. Plant Cell Physiol 45 (2004) 1779-1786
7. Yuasa K., Toyooka K., Fukuda H., and Matsuoka K. Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. Plant J 41 (2005) 81-94. The authors cloned a novel prolyl 4-hydroxylase, a type II integral membrane protein, from tobacco BY-2 cells. Their results indicated that basic amino acids in the amino-terminal cytoplasmic region of the protein play a role in its export from the ER. Its membrane-anchored nature is plant-specific, as integral membrane prolyl hydroxylases have not been found in other systems.
8. Phillipson B.A., Pimpl P., daSilva L.L., Crofts A.J., Taylor J.P., Movafeghi A., Robinson D.G., and Denecke J. Secretory bulk flow of soluble proteins is efficient and COPII dependent. Plant Cell 13 (2001) 2005-2020
9. Contreras I., Ortiz-Zapater E., and Aniento F. Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer. Plant J 38 (2004) 685-698
10. McCartney A.W., Dyer J.M., Dhanoa P.K., Kim P.K., Andrews D.W., McNew J.A., and Mullen R.T. Membrane-bound fatty acid desaturases are inserted co-translationally into the ER and contain different ER retrieval motifs at their carboxy termini. Plant J 37 (2004) 156-173
11. Hanton S.L., Bortolotti L.E., Renna L., Stefano G., and Brandizzi F. Crossing the divide - transport between the endoplasmic reticulum and Golgi apparatus in plants. Traffic 6 (2005) 267-277
12. Runions J., Brach T., Kuhner S., and Hawes C. Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J Exp Bot 57 (2006) 43-50. The authors studied protein flow within the membrane of the ER as it is continuously remodelled. Their results suggest that the ER moves actively over an actin scaffold. Tracking of Golgi movement demonstrated that individual stacks move at the same rate and in the same direction as ER-resident proteins, supporting the concept of a continuum between the ER, ERES and the Golgi apparatus.
13. Hawes C., and Satiat-Jeunemaitre B. The plant Golgi apparatus - going with the flow. Biochim Biophys Acta 1744 (2005) 465-480
14. Ritzenthaler C., Nebenführ A., Movafeghi A., Stussi-Garaud C., Behnia L., Pimpl P., Staehelin L.A., and Robinson D.G. Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera. Plant Cell 14 (2002) 237-261
15. Couchy I., Bolte S., Crosnier M.T., Brown S., and Satiat-Jeunemaitre B. Identification and localization of a β-COP-like protein involved in the morphodynamics of the plant Golgi apparatus. J Exp Bot 54 (2003) 2053-2063
16. Brandizzi F., Snapp E.L., Roberts A.G., Lippincott-Schwartz J., and Hawes C. Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell 14 (2002) 1293-1309
17. Short B., Haas A., and Barr F.A. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim Biophys Acta 1744 (2005) 383-395
18. Latijnhouwers M., Hawes C., and Carvalho C. Holding it all together? Candidate proteins for the plant Golgi matrix. Curr Opin Plant Biol 8 (2005) 632-639. This review discusses the current understanding of the golgin family of proteins in the context of a Golgi matrix. A comparison between plants and other systems attempts to identify putative plant homologues of candidate matrix proteins. This provides a starting point for further analyses of the structure and organization of the plant Golgi apparatus.
19. Renna L., Hanton S.L., Stefano G., Bortolotti L., Misra V., and Brandizzi F. Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein. Plant Mol Biol 58 (2005) 109-122
20. Latijnhouwers M., Hawes C., Carvalho C., Oparka K., Gillingham A.K., and Boevink P. An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds the small GTPase ARL1. Plant J 44 (2005) 459-470
21. Gilson P.R., Vergara C.E., Kjer-Nielsen L., Teasdale R.D., Bacic A., and Gleeson P.A. Identification of a Golgi-localised GRIP domain protein from Arabidopsis thaliana. Planta 219 (2004) 1050-1056
22. Stefano G., Renna L., Hanton S., Chatre L., Haas T.A., and Brandizzi F. ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix protein to the Golgi apparatus in plant cells. Plant Mol Biol 61 (2006) 431-449
23. Jürgens G. Membrane trafficking in plants. Annu Rev Cell Dev Biol 20 (2004) 481-504
24. Robinson D.G., Oliviusson P., and Hinz G. Protein sorting to the storage vacuoles of plants: a critical appraisal. Traffic 6 (2005) 615-625
25. daSilva L.L., Taylor J.P., Hadlington J.L., Hanton S.L., Snowden C.J., Fox S.J., Foresti O., Brandizzi F., and Denecke J. Receptor salvage from the prevacuolar compartment is essential for efficient vacuolar protein targeting. Plant Cell 17 (2005) 132-148
26. Oliviusson P., Heinzerling O., Hillmer S., Hinz G., Tse Y.C., Jiang L., and Robinson D.G. Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors. Plant Cell 18 (2006) 1239-1252. The authors identified a membrane-binding retromer-like protein complex in plants, which is localized to the prevacuolar compartment. The data presented in this paper suggest that cargo transport to the lytic compartment, and receptor cycling between the trans-Golgi network and the endosomal/prevacuolar compartments, is strongly conserved among eukaryotes.
27. daSilva L.L.P., Foresti O., and Denecke J. Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail. Plant Cell 18 (2006) 1477-1497. This paper demonstrates that both the transmembrane domain and the cytosolic tail of the plant vacuolar sorting receptor play a role in proper vacuolar targeting, indicating that multiple sequence motifs are necessary for its proper function. The mechanism of ER export of BP80, as well as the Golgi to prevacuolar compartment transport and recycling of this protein, is described.
28. Jolliffe N.A., Brown J.C., Neumann U., Vicre M., Bachi A., Hawes C., Ceriotti A., Roberts L.M., and Frigerio L. Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors. Plant J 39 (2004) 821-833
29. Pimpl P., Hanton S.L., Taylor J.P., Pinto-DaSilva L.L., and Denecke J. The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole. Plant Cell 15 (2003) 1242-1256
30. Xu J., and Scheres B. Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity. Plant Cell 17 (2005) 525-536
31. Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., and Sato M.H. Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells. Cell Struct Funct 29 (2004) 49-65
32. Saint-Jore-Dupas C., Gomord V., and Paris N. Protein localization in the plant Golgi apparatus and the trans-Golgi network. Cell Mol Life Sci 61 (2004) 159-171
33. Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., and Raikhel N.V. AtVPS45 complex formation at the trans-Golgi network. Mol Biol Cell 11 (2000) 2251-2265
34. Yoshino A., Bieler B.M., Harper D.C., Cowan D.A., Sutterwala S., Gay D.M., Cole N.B., McCaffery J.M., and Marks M.S. A role for GRIP domain proteins and/or their ligands in structure and function of the trans Golgi network. J Cell Sci 116 (2003) 4441-4454
35. Derby M.C., van Vliet C., Brown D., Luke M.R., Lu L., Hong W., Stow J.L., and Gleeson P.A. Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. J Cell Sci 117 (2004) 5865-5874
36. Villarejo A., Buren S., Larsson S., Dejardin A., Monne M., Rudhe C., Karlsson J., Jansson S., Lerouge P., Rolland N., et al. Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast. Nat Cell Biol 7 (2005) 1124-1131
37. Chen M.H., Huang L.F., Li H.M., Chen Y.R., and Yu S.M. Signal peptide-dependent targeting of a rice α-amylase and cargo proteins to plastids and extracellular compartments of plant cells. Plant Physiol 135 (2004) 1367-1377
38. Gutensohn M., Fan E., Frielingsdorf S., Hanner P., Hou B., Hust B., and Klosgen R.B. Toc, Tic, Tat et al.: structure and function of protein transport machineries in chloroplasts. J Plant Physiol 163 (2006) 333-347
39. Baker A., and Sparkes I.A. Peroxisome protein import: some answers, more questions. Curr Opin Plant Biol 8 (2005) 640-647
40. Sparkes I.A., Hawes C., and Baker A. AtPEX2 and AtPEX10 are targeted to peroxisomes independently of known endoplasmic reticulum trafficking routes. Plant Physiol 139 (2005) 690-700
41. Flynn C.R., Heinze M., Schumann U., Gietl C., and Trelease R.N. Compartmentalization of the plant peroxin, AtPex10p, within subdomain(s) of ER. Plant Sci 168 (2005) 635-652
42. Karnik S.K., and Trelease R.N. Arabidopsis peroxin 16 coexists at steady state in peroxisomes and endoplasmic reticulum. Plant Physiol 138 (2005) 1967-1981
43. Lisenbee C.S., Heinze M., and Trelease R.N. Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells. Plant Physiol 132 (2003) 870-882
44. Levitan A., Trebitsh T., Kiss V., Pereg Y., Dangoor I., and Danon A. Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum. Proc Natl Acad Sci USA 102 (2005) 6225-6230
45. McCartney A.W., Greenwood J.S., Fabian M.R., White K.A., and Mullen R.T. Localization of the tomato bushy stunt virus replication protein p33 reveals a peroxisome-to-endoplasmic reticulum sorting pathway. Plant Cell 17 (2005) 3513-3531
46. Takahashi H., Saito Y., Kitagawa T., Morita S., Masumura T., and Tanaka K. A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm. Plant Cell Physiol 46 (2005) 245-249
47. Oufattole M., Park J.H., Poxleitner M., Jiang L., and Rogers J.C. Selective membrane protein internalization accompanies movement from the endoplasmic reticulum to the protein storage vacuole pathway in Arabidopsis. Plant Cell 17 (2005) 3066-3080
48. Donaldson J.G., Honda A., and Weigert R. Multiple activities for Arf1 at the Golgi complex. Biochim Biophys Acta 1744 (2005) 364-373
49. Segui-Simarro J.M., and Staehelin L.A. Cell cycle-dependent changes in Golgi stacks, vacuoles, clathrin-coated vesicles and multivesicular bodies in meristematic cells of Arabidopsis thaliana: a quantitative and spatial analysis. Planta 223 (2006) 223-236
50. Espenshade P.J. SREBPs: sterol-regulated transcription factors. J Cell Sci 119 (2006) 973-976
51. Benghezal M., Wasteneys G.O., and Jones D.A. The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants. Plant Cell 12 (2000) 1179-1201
52. Denecke J., De Rycke R., and Botterman J. Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J 11 (1992) 2345-2355