Protein transport within the plant cell endomembrane system: An update

Current Opinion in Plant Biology

Volumn 1, Issue 6, 1998, Pages 463-469

  Matsuoka, Ken ^a   Bednarek, Sebastian Y ^b  

^a NAGOYA UNIVERSITY   (Japan)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; MESSENGER RNA; VEGETABLE PROTEIN;

CELL COMPARTMENTALIZATION; CELL FRACTIONATION; CELL MEMBRANE; CEREAL; ENDOCYTOSIS; GENETICS; METABOLISM; PLANT SEED; PRENATAL DEVELOPMENT; REVIEW; TRANSPORT AT THE CELLULAR LEVEL;

BIOLOGICAL TRANSPORT; CELL COMPARTMENTATION; CELL MEMBRANE; CEREALS; ENDOCYTOSIS; MOLECULAR CHAPERONES; PLANT PROTEINS; RNA, MESSENGER; SEEDS; SUBCELLULAR FRACTIONS;

EID: 0032240929     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(98)80036-8     Document Type: Article

References (10)

1. Bassham DC, Raikhel NV: Transport proteins in the plasma membrane and the secretory system. Trends Plant Sci 1996, 1:15-20.
2. Okita T, Rogers J: Compartmentation of proteins in the endomembrane system of plant cells. Annu Rev Plant Physiol Plant Mol Biol 1996, 47:327-350.
3. Okita TW, Choi SB, Ito H, Muench DG, Wu Y, Zhang F: Entry into the secretory system - the role of mRNA localization. J Exp Bot 1998, 49:1081-1089.
4. Ceriotti A, Duranti M, Bollini R: Effects of N-glycosylation on the folding and structure of plant proteins. J Exp Bot 1998. 49:1091-1103.
5. Muench DG, Wu Y, Coughlan SJ, Okita TW: Evidence for a cytoskeleton-associated binding site involved in prolamine mRNA localization to the protein bodies in rice endosperm tissue. Plant Physiol 1998, 116:559-569. Rice prolamin and glutelin mRNAs are localized to morphologically distinct parts of the ER. In this paper, PB associated polysomes were found to be resistant to detergent extraction and puromycin treatment suggesting that the majority of prolamine mRNA is not directly anchored to the ER membrane through ribosome binding sites nor through the binding of the nascent prolamin polypeptide. Rather, the prolamine polysome-binding activity was shown to be associated with cytoskeletal elements.
6. Clore AM, Dannenhoffer JM, Larkins BA: EF-1-alpha is associated with a cytoskeletal network surrounding protein bodies in maize endosperm cells. Plant Cell 1996, 8:2003-2014.
7. Coleman CE, Herman EM, Takasaki K, Larkins BA: The maize γ-zein sequesters α-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 1996, 8:2335-2345.
8. Bagga S, Adams HP, Rodriguez FD, Kemp JD, Sengupta-Gopalan C: Coexpression of the maize δ-zein and β-zein genes results in stable accumulation of δ-zein in endoplasmic reticulum-derived protein bodies formed by β-zein. Plant Cell 1997, 9:1683-1696. Zeins, the major seed storage proteins of maize, are synthesized on the rER and are deposited in ER-PB. In this paper β-zein and δ-zein were shown to be stably expressed and deposited in zein-specific ER-PB in transgenic tobacco leaves. Coexpression of β-zein and δ-zein together resulted in an increase in δ-zein accumulation relative to plants expressing d-zein alone and both proteins colocalized in the same PB. These results suggest that δ-zein interacts with and stabilizes the assembly of δ-zein into PB.
9. Gillikin JW, Zhang F, Coleman CE, Bass HW, Larkins BA, Boston RS: A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane. Plant Physiol 1997, 114:345-352.
10. Coleman CE, Clore AM, Ranch JP, Higgins R, Lopes MA, Larkins, BA: Expression of a mutant alpha-zein creates the floury2 phenotype in transgenic maize. Proc Natl Acad Sci USA 1997, 94:7094-7097.