Cis-elements of protein transport to the plant vacuoles

被引:90
作者
Matsuoka, K
Neuhaus, JM
机构
[1] Univ Neuchatel, Biochim Lab, CH-2007 Neuchatel 7, Switzerland
[2] Nagoya Univ, Grad Sch Bioagr Sci, Biochem Lab, Chikusa Ku, Nagoya, Aichi 4648601, Japan
关键词
protein trafficking; propeptides; vacuole; tonoplast; sorting receptor;
D O I
10.1093/jexbot/50.331.165
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Vacuolar proteins are synthesized and translocated into the endoplasmic reticulum and transported to the vacuoles through the secretory pathway. Three different types of vacuolar sorting signals have been identified, carried by N- or C-terminal propeptides or internal sequences. These signals are needed to target proteins to the different types of vacuoles that can coexist in a single plant cell. A conserved motif (NPIXL or NPIR) was identified within N-terminal propeptides, but can also function in a C-terminal propeptide and targets proteins in a receptor-mediated manner to a lytic vacuole. Binding to a family of putative sorting receptors for sequence-specific vacuolar sorting signals has been used as an assay to identify further peptides with other binding motifs. No motif was found in C-terminal sorting sequences, which need an accessible terminus, suggesting that they are recognized from the end by a still unknown receptor, The phosphatidylinositol kinase inhibitor wortmannin differentially affects sorting mediated by these two sorting sequences, suggesting different sorting mechanisms, Less is known about sorting mediated by internal protein sequences, which do not contain the conserved motif identified in N-terminal propeptides and may function by aggregation, leading to transport by coat-less dense vesicles to protein storage vacuoles, Even less is known about the sorting of tonoplast proteins, for which several sorting systems will also be needed.
引用
收藏
页码:165 / 174
页数:10
相关论文
共 57 条
[2]   BEYOND BULK FLOW [J].
BALCH, WE ;
FARQUHAR, MG .
TRENDS IN CELL BIOLOGY, 1995, 5 (01) :16-19
[3]   Membrane dynamics at the endoplasmic reticulum Golgi interface [J].
Bannykh, SI ;
Balch, WE .
JOURNAL OF CELL BIOLOGY, 1997, 138 (01) :1-4
[4]   The secretory pathway of protists: Spatial and functional organization and evolution [J].
Becker, B ;
Melkonian, M .
MICROBIOLOGICAL REVIEWS, 1996, 60 (04) :697-+
[5]  
Conceicao ADS, 1997, PLANT CELL, V9, P571, DOI 10.2307/3870508
[6]   Specific accumulation of GFP in a non-acidic vacuolar compartment via a C-terminal propeptide-mediated sorting pathway [J].
Di Sansebastiano, GP ;
Paris, N ;
Marc-Martin, S ;
Neuhaus, JM .
PLANT JOURNAL, 1998, 15 (04) :449-457
[7]   DETERMINATION OF THE FUNCTIONAL ELEMENTS WITHIN THE VACUOLAR TARGETING SIGNAL OF BARLEY LECTIN [J].
DOMBROWSKI, JE ;
SCHROEDER, MR ;
BEDNAREK, SY ;
RAIKHEL, NV .
PLANT CELL, 1993, 5 (05) :587-596
[8]  
FREYDL E, 1995, THESIS U BASEL
[9]  
GOMEZ L, 1993, PLANT CELL, V5, P1113, DOI 10.1105/tpc.5.9.1113
[10]   The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER [J].
Gomord, V ;
Denmat, LA ;
FitchetteLaine, AC ;
SatiatJeunemaitre, B ;
Hawes, C ;
Faye, L .
PLANT JOURNAL, 1997, 11 (02) :313-325