Plant Cell EPICENTRE Biotechnologies
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via ISI Web of Science (40)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Frigerio, L.
Right arrow Articles by Vitale, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Frigerio, L.
Right arrow Articles by Vitale, A.
Agricola
Right arrow Articles by Frigerio, L.
Right arrow Articles by Vitale, A.
Plant Cell, Vol. 13, 1109-1126, May 2001, Copyright © 2001, American Society of Plant Physiologists

Influence of KDEL on the Fate of Trimeric or Assembly-Defective Phaseolin: Selective Use of an Alternative Route to Vacuoles

Lorenzo Frigerioa,b, Alessandra Pastresa, Alessandra Pradaa, and Alessandro Vitalea
a Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, 20133 Milano, Italy
b Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom

Correspondence to: Alessandro Vitale, vitale{at}ibv.mi.cnr.it (E-mail), 39-02-23699411 (fax)

The tetrapeptide KDEL is commonly found at the C terminus of soluble proteins of the endoplasmic reticulum (ER), and it contributes to their localization by interacting with a receptor that recycles between the Golgi complex and the ER. We investigated the effects of the addition of KDEL to phaseolin, a protein normally delivered from the ER to storage vacuoles via the Golgi complex. We show that KDEL prevents acquisition of trans-Golgi–specific glycan modifications and causes interactions with the chaperone BiP that are distinct from the ones between BiP and defective proteins. KDEL markedly increases the stability of phaseolin, but a small proportion of phaseolin-KDEL slowly reaches the vacuole without undergoing Golgi-mediated glycan modifications, in a process that can be inhibited by brefeldin A but not monensin. Our results indicate that KDEL can operate with high efficiency before proteins can reach the late Golgi cisternae but allows or promotes delivery to vacuoles via an alternative mechanism. However, addition of KDEL does not alter the destiny of an assembly-defective form of phaseolin, suggesting that the plant ER quality control mechanism is dominant over KDEL effects.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
K. L. Chamberlain, R. S. Marshall, N. A. Jolliffe, L. Frigerio, A. Ceriotti, J. M. Lord, and L. M. Roberts
Ricin B Chain Targeted to the Endoplasmic Reticulum of Tobacco Protoplasts Is Degraded by a CDC48- and Vacuole-independent Mechanism
J. Biol. Chem., November 28, 2008; 283(48): 33276 - 33286.
[Abstract] [Full Text] [PDF]

Home page
 Mol PlantHome page
O. Foresti, F. De Marchis, M. de Virgilio, E. M. Klein, S. Arcioni, M. Bellucci, and A. Vitale
Protein Domains Involved in Assembly in the Endoplasmic Reticulum Promote Vacuolar Delivery when Fused to Secretory GFP, Indicating a Protein Quality Control Pathway for Degradation in the Plant Vacuole
Mol Plant, November 1, 2008; 1(6): 1067 - 1076.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. de Virgilio, F. De Marchis, M. Bellucci, D. Mainieri, M. Rossi, E. Benvenuto, S. Arcioni, and A. Vitale
The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin
J. Exp. Bot., July 1, 2008; 59(10): 2815 - 2829.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
M. Leroch, H. E. Neuhaus, S. Kirchberger, S. Zimmermann, M. Melzer, J. Gerhold, and J. Tjaden
Identification of a Novel Adenine Nucleotide Transporter in the Endoplasmic Reticulum of Arabidopsis
PLANT CELL, February 1, 2008; 20(2): 438 - 451.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
P. R. Hunter, C. P. Craddock, S. Di Benedetto, L. M. Roberts, and L. Frigerio
Fluorescent Reporter Proteins for the Tonoplast and the Vacuolar Lumen Identify a Single Vacuolar Compartment in Arabidopsis Cells
Plant Physiology, December 1, 2007; 145(4): 1371 - 1382.
[Abstract] [Full Text] [PDF]

Home page
 CVIHome page
X.-M. Lou, Q.-H. Yao, Z. Zhang, R.-H. Peng, A.-S. Xiong, and H.-K. Wang
Expression of the Human Hepatitis B Virus Large Surface Antigen Gene in Transgenic Tomato Plants
Clin. Vaccine Immunol., April 1, 2007; 14(4): 464 - 469.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. K. Min, S. J. Kim, Y. Miao, J. Shin, L. Jiang, and I. Hwang
Overexpression of Arabidopsis AGD7 Causes Relocation of Golgi-Localized Proteins to the Endoplasmic Reticulum and Inhibits Protein Trafficking in Plant Cells
Plant Physiology, April 1, 2007; 143(4): 1601 - 1614.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
K. Fuji, T. Shimada, H. Takahashi, K. Tamura, Y. Koumoto, S. Utsumi, K. Nishizawa, N. Maruyama, and I. Hara-Nishimura
Arabidopsis Vacuolar Sorting Mutants (green fluorescent seed) Can Be Identified Efficiently by Secretion of Vacuole-Targeted Green Fluorescent Protein in Their Seeds
PLANT CELL, February 1, 2007; 19(2): 597 - 609.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
M. Park, D. Lee, G.-J. Lee, and I. Hwang
AtRMR1 functions as a cargo receptor for protein trafficking to the protein storage vacuole
J. Cell Biol., August 29, 2005; 170(5): 757 - 767.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
S. Castelli and A. Vitale
The phaseolin vacuolar sorting signal promotes transient, strong membrane association and aggregation of the bean storage protein in transgenic tobacco
J. Exp. Bot., May 1, 2005; 56(415): 1379 - 1387.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
L. Achnine, E. B. Blancaflor, S. Rasmussen, and R. A. Dixon
Colocalization of L-Phenylalanine Ammonia-Lyase and Cinnamate 4-Hydroxylase for Metabolic Channeling in Phenylpropanoid Biosynthesis
PLANT CELL, November 1, 2004; 16(11): 3098 - 3109.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
E. Arcalis, S. Marcel, F. Altmann, D. Kolarich, G. Drakakaki, R. Fischer, P. Christou, and E. Stoger
Unexpected Deposition Patterns of Recombinant Proteins in Post-Endoplasmic Reticulum Compartments of Wheat Endosperm
Plant Physiology, November 1, 2004; 136(3): 3457 - 3466.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
D. Mainieri, M. Rossi, M. Archinti, M. Bellucci, F. De Marchis, S. Vavassori, A. Pompa, S. Arcioni, and A. Vitale
Zeolin. A New Recombinant Storage Protein Constructed Using Maize {gamma}-Zein and Bean Phaseolin
Plant Physiology, November 1, 2004; 136(3): 3447 - 3456.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. Park, S. J. Kim, A. Vitale, and I. Hwang
Identification of the Protein Storage Vacuole and Protein Targeting to the Vacuole in Leaf Cells of Three Plant Species
Plant Physiology, February 1, 2004; 134(2): 625 - 639.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
O. Foresti, L. Frigerio, H. Holkeri, M. de Virgilio, S. Vavassori, and A. Vitale
A Phaseolin Domain Involved Directly in Trimer Assembly Is a Determinant for Binding by the Chaperone BiP
PLANT CELL, October 1, 2003; 15(10): 2464 - 2475.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
T. Okamoto, T. Shimada, I. Hara-Nishimura, M. Nishimura, and T. Minamikawa
C-Terminal KDEL Sequence of A KDEL-Tailed Cysteine Proteinase (Sulfhydryl-Endopeptidase) Is Involved in Formation of KDEL Vesicle and in Efficient Vacuolar Transport of Sulfhydryl-Endopeptidase
Plant Physiology, August 1, 2003; 132(4): 1892 - 1900.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
J. L. Hadlington, A. Santoro, J. Nuttall, J. Denecke, J. K-C. Ma, A. Vitale, and L. Frigerio
The C-terminal Extension of a Hybrid Immunoglobulin A/G Heavy Chain Is Responsible for Its Golgi-mediated Sorting to the Vacuole
Mol. Biol. Cell, June 1, 2003; 14(6): 2592 - 2602.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
F. Brandizzi, E. L. Snapp, A. G. Roberts, J. Lippincott-Schwartz, and C. Hawes
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, June 1, 2002; 14(6): 1293 - 1309.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
A. A. Zamyatnin Jr,, A. G. Solovyev, A. A. Sablina, A. A. Agranovsky, L. Katul, H. J. Vetten, J. Schiemann, A. E. Hinkkanen, K. Lehto, and S. Yu. Morozov
Dual-colour imaging of membrane protein targeting directed by poa semilatent virus movement protein TGBp3 in plant and mammalian cells
J. Gen. Virol., March 1, 2002; 83(3): 651 - 662.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
B. A. Phillipson, P. Pimpl, L. L. P. daSilva, A. J. Crofts, J. P. Taylor, A. Movafeghi, D. G. Robinson, and J. Denecke
Secretory Bulk Flow of Soluble Proteins Is Efficient and COPII Dependent
PLANT CELL, September 1, 2001; 13(9): 2005 - 2020.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
K. Tormakangas, J. L. Hadlington, P. Pimpl, S. Hillmer, F. Brandizzi, T. H. Teeri, and J. Denecke
A Vacuolar Sorting Domain May Also Influence the Way in Which Proteins Leave the Endoplasmic Reticulum
PLANT CELL, September 1, 2001; 13(9): 2021 - 2032.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 2001 by the American Society of Plant Biologists