Endomembranes and vesicle trafficking

Current Opinion in Plant Biology

Volumn 2, Issue 6, 1999, Pages 454-461

  Hawes, Chris R ^a   Brandizzi, Federica ^a   Andreeva, Alexandra V ^a  

^a OXFORD BROOKES UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033485551     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(99)00023-0     Document Type: Review

References (53)

1. Galili G., Sengupta-Gopalan C., Ceriotti A. The endoplasmic reticulum of plant cells and its role in protein maturation and biogenesis of oil bodies. Plant Mol Biol. 38:1998;1-29.
2. Møgelsvang S., Simpson D.J. Protein folding and transport from the endoplasmic reticulum to the Golgi apparatus in plants. J Plant Physiol. 153:1998;1-15.
3. Vitale A., Denecke J. The endoplasmic reticulum - gateway of the secretory pathway. Plant Cell. 11:1999;615-628.
4. Andreeva A.V., Kutuzov M.A., Evans D.E., Hawes C.R. Plant Golgi apparatus: one hundred years of questions. J Exp Bot. 49:1998;1281-1291.
5. Dupree P., Sherrier D.J. The plant Golgi apparatus. Biochim Biophys Acta. 1404:1998;259-270.
6. Beevers L., Raikhel N.V. Transport to the vacuole: receptors and trans elements. J Exp Bot. 41:1998;1271-1279.
7. Herman E.M., Larkins B.A. Protein storage bodies and vacuoles. Plant Cell. 11:1999;601-613.
8. Marty F. Plant vacuoles. Plant Cell. 11:1999;587-599.
9. Matsuoka K., Neuhaus J.M. Cis-elements of protein transport to the plant vacuoles. J Exp Bot. 50:1999;165-174.
10. Neuhaus J.M., Rogers J.C. Sorting of proteins to vacuoles in plant cells. Plant Mol Biol. 38:1998;127-144.
11. Robinson D.G., Galili G., Herman E., Hillmer S. Topical aspects of vacuolar protein transport: autophagy and prevacuolar compartments. J Exp Bot. 49:1998;1263-1270.
12. Robinson D.G., Baumer M., Hinz G., Hohl I. Vesicle transfer of storage proteins to the vacuole: the role of the Golgi apparatus and multivesicular bodies. J Plant Physiol. 152:1998;659-667.
13. Rogers J.C. Compartmentation of plant cell proteins in separate lytic and protein storage vacuoles. J Plant Physiol. 152:1998;653-658.
14. Vitale A., Raikhel N.V. What do proteins need to reach different vacuoles? Trends Plant Sci. 4:1999;149-155.
15. Battey N.H., James N.C., Greenland A.J., Brownlee C. Exocytosis and endocytosis. Plant Cell. 11:1999;643-659.
16. Thiel G., Battey N.H. Exocytosis in plants. Plant Mol Biol. 38:1998;111-125.
17. Robinson D.G., Hintz G., Holstein S.E.H. The molecular characterization of transport vesicles. Plant Mol Biol. 38:1998;49-76.
18. Pagny S., Lerouge P., Faye L., Gomord V. Signals and mechanisms for protein retention in the endoplasmic reticulum. J Exp Bot. 50:1999;157-164.
19. Hara-Nishimura I., Schimada T., Hatano K., Takeuchi Y., Nishimura M. Transport of storage proteins to protein storage vacuoles is mediated by large precursor accumulating vesicles. Plant Cell. 10:1998;825-836.
20. MacRobbie E.A.C. Vesicle trafficking: a role in trans-tonoplast ion movements? J Exp Bot. 50:1999;925-934.
21. +-ATPase in carrot protoplasts may serve to adjust the number of proton pumps at the plasma membrane or to monitor their functional condition.
22. Homann U. Fusion and fission of plasma-membrane material accommodates for osmotically induced changes in the surface area of guard cell protoplasts. Planta. 206:1998;329-333.
23. Homann U., Tester M. Patch clamp capacitance measurements to study exocytosis and endocytosis. Trends Plant Sci. 3:1998;110-114.
24. Thiel G., Kreft M., Zorec R. Unitary exocytotic and endocytotic events in Zea mays L. coleoptile protoplasts. Plant J. 13:1998;117-120. Using cell-attached capacitance measurements, the authors were able to distinguish between single endocytic and exocytotic events and have quantified the rate of single endocytic events in Zea mays coleoptile protoplasts, which has been estimated as 1.5±1.4 events/min.
25. 2+ concentrations. The authors conclude that exocytosis from root cap protoplasts is more similar to regulated exocytosis but cannot be categorised as regulated or constitutive as it has some features in common with both pathways.
26. Hayashi M., Toriyama K., Kondo M., Hara-Nishimura I., Nishimura M. Accumulation of a fusion protein containing 2S albumin induces novel vesicles in vegetative cells of Arabidopsis. Plant Cell Physiol. 40:1999;263-272. Ectopic expression of 2S albumin in Arabidopsis thaliana was found to induce precursor-accumulating (PAC) vesicles in vegetative cells. PAC vesicles are normally observed exclusively in developing seeds. This demonstrates that the presence of a particular protein may serve as a signal sufficient to induce the pathway necessary for its transport.
27. Frigerio L., de Virgilio M., Prada A., Faoro F., Vitale A. Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide. Plant Cell. 10:1998;1031-1042. This work demonstrates that vacuolar sorting of phaseolin, a storage protein from common bean, can be saturated by phaseolin overexpression, and the 'excess' protein is re-routed towards secretion. The carboxy-terminal tetrapeptide of phaseolin is identified as a signal necessary for its vacuolar targeting.
28. Bischoff F., Molendijk A., Rajendrakumar C.S.V., Palme K GTP-binding proteins in plants. Cell Mol Life Sci. 55:1999;233-256.
29. Sanderfoot A.A., Raikhel N.V. The specificity of vesicle trafficking: coat proteins and SNAREs. Plant Cell. 11:1999;629-641.
30. Crofts A.J., Denecke J. Calreticulin and calnexin in plants. Trends Plant Sci. 3:1998;396-399.
31. Leborgne-Castel N., Jelitto-Van Dooren E.P.W.M., Crofts A.J., Denecke J. Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress. Plant Cell. 11:1999;459-469.
32. Lerouge P., Cabanes-Macheteau M., Rayon C., Fichette-Laine A.C., Gomord V., Faye L. N-glycoprotein biosynthesis in plants: recent developments and future trends. Plant Mol Biol. 38:1998;31-48.
33. Neckelmann G., Orellana A. Metabolism of uridine 5′-diphosphate-glucose in Golgi vesicles from pea stems. Plant Physiology. 117:1998;1007-1014.
34. Perrin R.M., DeRocher A.E., Bar-Peled M., Zeng W., Norambuena L., Orellana A., Raikhel N.V., Keegstra K. Xyloglucan fucosyltransferase, an enzyme involved in plant cell wall biosynthesis. Science. 284:1999;1976-1979. This is the first work reporting cloning of a plant glycosyltransferase putatively resident in the Golgi apparatus. Previous attempts to clone these enzymes using corresponding sequences from mammals and bacteria have been unsuccessful due to the low sequence conservation between Golgi glycosyltransferases. A 60 kDa fucosyltransferase was purified from pea epicotyls; the partial sequence information allowed cloning of its homologue from Arabidopsis. The recombinant protein expressed in mammalian COS cells was found to be functionally active.
35. Wee E.G.T., Sherrier D.J., Prime T.A., Dupree P. Targeting of active sialyltransferase to the plant Golgi apparatus. Plant Cell. 10:1998;1759-1768. The authors expressed a gene encoding myc-tagged rat sialyltransferase in Aarabidopsis thaliana and demonstrated, using biochemical analysis, immunocytochemistry and immunogold labelling, that the recombinant protein is active and localised to trans-Golgi. These data support the model of retention of specific Golgi proteins on the basis of the length of their transmembrane domains, as opposed to the model of 'kin recognition'.
36. Palacpac N.Q., Yoshida S., Sakai H., Kimura Y., Fujiyama K., Yoshida T., Seki T. Stable expression of human 1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc Natl Acad Sci USA. 96:1998;4692-4697. The article reports on successful expression of the gene encoding human β1,4-galactosyltransferase in tobacco BY2 cells, which resulted in galactosylation of about half of the plant N-glycans. This demonstrates that it is possible, in principle, to modify N-glycosylation pathways of plant cells and provides a potential marker for the plant Golgi apparatus.
37. Jiang L., Rogers J.C. Functional analysis of a Golgi-localized Kex2p like protease in tobacco suspension culture cells. Plant J. 18:1999;23-32. A chimeric reporter protein containing Kex2 cleavage sites was used to demonstrate that a plant protease with a Kex2-like specificity is localised to the Golgi apparatus or post-Golgi compartments. This work provides a new biochemical marker to study protein transport through the plant Golgi apparatus. Such studies could help to elucidate the bifurcation of pathways leading to storage/lytic vacuoles.
38. Boevink P., Martin B., Oparka K., Santa Cruz S., Hawes C. Transport of virally expressed green fluorescent protein through the secretory pathway in tobacco leaves is inhibited by cold shock and brefeldin A. Planta. 208:1999;392-400. Green fluorescent proteins (GFP) with a sporamin signal peptide with or without KDEL were located in the endoplasmic reticulum or secreted, respectively. After brefeldin A or cold treatment (i.e. a secretion blockage) secreted GFP was also found in endoplasmic reticulum.
39. Di Sansebastiano G.P., Paris N., MarcMartin S., Neuhaus J.M. Specific accumulation of GFP in a non-acidic vacuolar compartment via a C-terminal propeptide-mediated sorting pathway. Plant J. 15:1998;449-457. The authors developed a vacuolar form of green fluorescent protein (GFP) that specifically targets non-acidic vacuoles, providing an easy way to discriminate between different vacuole types in vivo.
40. Boevink P., Oparka K., Santa Cruz S., Martin B., Betteridge A., Hawes C. Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15:1998;441-447. Two constructs (encoding green fluorescent protein fused to either the transmembrane domain of rat sialyl transferase or Arabidopsis ERD2) expressed in the potato virus X (PVX) vector were used to show a close spatial relationship between the endoplasmic reticulum (ER) and Golgi in vivo in leaf epidermal cells of Nicotiana clevelandii. Golgi stacks rapidly moved along the cortical ER network without moving off the ER tubules. The Golgi movement was dependent on the actin cytoskeleton that matched precisely the architecture of the ER network. This work reinforced the question of how transfer between the Golgi and ER occurs. Brefeldin A induced retrograde transport of the chimeric Golgi membrane proteins to the ER.
41. Andreeva A.V., Kutuzov M.A., Evans D.E., Hawes C.R. Proteins involved in membrane transport between the ER and the Golgi apparatus: 21 putative plant homologues revealed by dbEST searching. Cell Biol Int. 22:1998;145-160.
42. Movafeghi A., Happel N., Pimpl P., Tai G.H., Robinson D.G. Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles. Plant Physiol. 119:1999;1437-1445. This is one of the first practical steps towards demonstrating the existence of COP-coated vesicles in plants, which has not been proved experimentally so far. Antisera against Arabidopsis Sec21p and Arabidopsis Sec23p were found to recognise the homologs of these proteins in Brassica oleracea and were used for their immunolocalisation. The results are in line with the notion that COPII vesicles are formed at the endoplasmic reticulum, whereas COPI vesicles can be made by both Golgi and endoplasmic reticulum membranes.
43. Takeuchi M., Tada M., Saito C., Yashiroda H., Nakano A. Isolation of a tobacco cDNA encoding Sar1 GTPase and analysis of its dominant mutations in vesicular traffic using a yeast complementation system. Plant Cell Physiol. 39:1998;590-599.
44. De Ruijter N.C.A., Emons A.M.C. Actin-binding proteins in plant cells. Plant Biol. 1:1999;26-35.
45. Kuriyama H., Takano H., Suzuki L., Uchida H., Kawano S., Kuroiwa H., Kuroiwa T. Characterization of Chlamydomonas reinhardtii zygote-specific cDNAs that encode novel proteins containing ankyrin repeats and WW domains. Plant Physiol. 119:1999;873-884.
46. 14]acetate, the presence of sterols was compared in endoplasmic-reticulum-, Golgi apparatus- and plasma membrane-enriched fractions. The results demonstrate the active transport of sterols from the endoplasmic reticulum to the plasma membrane, which is inhibited by low temperatures, monensin and brefeldin A. This indicates probable involvement of the Golgi apparatus in the membrane-mediated transport of sterols to the plasma membrane.
47. Sturbois-Balcerzak B., Vincent P., Maneta-Peyret L., Duvert M., Satiat Jeunemaitre B., Cassagne C., Moreau P. ATP-dependent formation of phosphatidylserine-rich vesicles from the endoplasmic reticulum of leek cells. Plant Physiol. 120:1999;245-256. This article documents the formation of small (70-80 nm) phosphatidylserine-enriched vesicles from the endoplasmic reticulum (ER) in leek. Vesicle formation requires ATP and is inhibited by its non-hydrolysable analogue ATPγS. This data substantiates the evidence for the vesicular pathway of phosphatidylserine transport to the plasma membrane and provides the first example of phospholipid sorting from plant ER to ER-derived vesicles.
48. Kearns M.A., Monks D.E., Fang M., Rivas M.P., Courtney P.D., Chen J., Prestwich G.D., Theibert A.B., Dewey R.E., Bankaitis V.A. Novel developmentally regulated phosphoinositide binding proteins from soybean whose expression bypasses the requirement for an essential phosphatidylinositol transfer protein in yeast. EMBO J. 17:1998;4004-4017.
49. - channel response to abscisic acid (ABA) in guard cells. The role of this syntaxin in ABA signalling is discussed. This is the first evidence for a direct link between vesicular trafficking machinery and a hormone signal transduction pathway.
50. Winicur Z.M., Zhang G.F., Staehelin L.A. Auxin deprivation induces synchronous Golgi differentiation in suspension-cultured tobacco BY2 cells. Plant Physiol. 117:1998;501-513. The authors found that auxin deprivation induces differentiation of suspension-cultured BY2 into cells resembling slime-secreting cells of the root cap. This is accompanied by morphological changes in the Golgi stacks, appearance of arabinogalactan proteins in the Golgi apparatus detectable by the JIM13 antibody and changes in the secretion of general tissue differentiation markers. This finding can be used to manipulate the secretory activity of BY2 cells and the organisation of the Golgi apparatus in a reproducible manner.
51. Strasser R., Mucha J., Schwihla H., Altmann F., Glossi J., Steinkellner H. Molecular cloning and characterization of cDNA coding for beta 1,2N-acetylglucosaminyltransferase I (GlcNAc-TI) from Nicotiana tabacum. Glycobiology. 9:1999;779-785.
52. Bakker D., Lommen A., Jordi W., Stiekema W., Bosch D. An Arabidopsis thaliana cDNA complements the N-acetylglucosaminyltransferase I deficiency of CHO Lec1 cells. Biochem Biophys Res Commun. 261:1999;829-832.
53. Essl D., Dirnberger D., Gomord V., Strasser R., Faye L., Glossl J., Steinkellner H. The N-terminal 77 amino acids from tobacco N-acetylglucosaminyltransferase I are sufficient to retain a reporter protein in the Golgi apparatus of Nicotiana benthamiana cells. FEBS Lett. 453:1999;169-173.