The endoplasmic reticulum of plant cells and its role in protein maturation and biogenesis of oil bodies

被引:72
作者
Galili, G [1 ]
Sengupta-Gopalan, C
Ceriotti, A
机构
[1] Weizmann Inst Sci, Dept Plant Sci, IL-76100 Rehovot, Israel
[2] New Mexico State Univ, Dept Agron & Hort, Las Cruces, NM 88003 USA
[3] CNR, Ist Biosintesi Vegetali, I-20133 Milan, Italy
关键词
plants; endoplasmic reticulum; molecular chaperones; quality control; protein bodies; lipid bodies;
D O I
10.1023/A:1006011919671
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The endoplasmic reticulum (ER) is the port of entry of proteins into the endomembrane system, and it is also involved in lipid biosynthesis and storage. This organelle contains a number of soluble and membrane-associated enzymes and molecular chaperones, which assist the folding and maturation of proteins and the deposition of lipid storage compounds. The regulation of translocation of proteins into the ER and their subsequent maturation within the organelle have been studied in detail in mammalian and yeast cells, and more recently also in plants. These studies showed that in general the functions of the ER in protein synthesis and maturation have been highly conserved between the different organisms. Yet, the ER of plants possesses some additional functions not found in mammalian and yeast cells. This compartment is involved in cell to cell communication via the plasmodesmata, and, in specialized cells, it serves as a storage site for proteins. The plant ER is also equipped with enzymes and structural proteins which are involved in the process of oil body biogenesis and lipid storage. In this review we discuss the components of the plant ER and their function in protein maturation and biogenesis of oil bodies. Due to the large number of cited papers, we were not able to cite all individual references and in many cases we refer the readers to reviews and references therein. We apologize to the authors whose references are not cited.
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页码:1 / 29
页数:29
相关论文
共 276 条
[31]   Interaction of rice and human SRP19 polypeptides with signal recognition particle RNA [J].
Chittenden, K ;
Gowda, K ;
Black, SD ;
Zwieb, C .
PLANT MOLECULAR BIOLOGY, 1997, 34 (03) :507-515
[32]  
CHRISPEELS MJ, 1991, ANNU REV PLANT PHYS, V42, P21, DOI 10.1146/annurev.pp.42.060191.000321
[33]   A DEFECTIVE SIGNAL PEPTIDE IN THE MAIZE HIGH-LYSINE MUTANT FLOURY-2 [J].
COLEMAN, CE ;
LOPES, MA ;
GILLIKIN, JW ;
BOSTON, RS ;
LARKINS, BA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (15) :6828-6831
[34]   The maize gamma-zein sequesters alpha-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm [J].
Coleman, CE ;
Herman, EM ;
Takasaki, K ;
Larkins, BA .
PLANT CELL, 1996, 8 (12) :2335-2345
[35]   3,4-DEHYDROPROLINE INHIBITS CELL-WALL ASSEMBLY AND CELL-DIVISION IN TOBACCO PROTOPLASTS [J].
COOPER, JB ;
HEUSER, JE ;
VARNER, JE .
PLANT PHYSIOLOGY, 1994, 104 (02) :747-752
[36]  
CORAGGIO I, 1988, EUR J CELL BIOL, V47, P165
[37]   Cloning and characterization of the calreticulin gene from Ricinus communis L. [J].
Coughlan, SJ ;
Hastings, C ;
Winfrey, R .
PLANT MOLECULAR BIOLOGY, 1997, 34 (06) :897-911
[38]   TRANSCRIPTIONAL INDUCTION OF GENES ENCODING ENDOPLASMIC-RETICULUM RESIDENT PROTEINS REQUIRES A TRANSMEMBRANE PROTEIN-KINASE [J].
COX, JS ;
SHAMU, CE ;
WALTER, P .
CELL, 1993, 73 (06) :1197-1206
[39]   The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane [J].
Cox, JS ;
Chapman, RE ;
Walter, P .
MOLECULAR BIOLOGY OF THE CELL, 1997, 8 (09) :1805-1814
[40]   A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response [J].
Cox, JS ;
Walter, P .
CELL, 1996, 87 (03) :391-404