The PRA1 gene family in Arabidopsis

被引:40
作者
Alvim Kamei, Claire Lessa [1 ,2 ,3 ]
Boruc, Joanna [1 ,3 ]
Vandepoele, Klaas [1 ,3 ]
Van den Daele, Hilde [1 ,3 ]
Maes, Sara [1 ,3 ]
Russinova, Eugenia [1 ,3 ]
Inze, Dirk [1 ,3 ]
De Veylder, Lieven [1 ,3 ]
机构
[1] Univ Ghent VIB, Dept Plant Syst Biol, B-9052 Ghent, Belgium
[2] Univ Fed Rio de Janeiro, Inst Bioquim Med, BR-21941590 Rio De Janeiro, Brazil
[3] Univ Ghent, Dept Mol Genet, B-9052 Ghent, Belgium
关键词
D O I
10.1104/pp.108.122226
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis ( Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.
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收藏
页码:1735 / 1749
页数:15
相关论文
共 61 条
[1]   PRA isoforms are targeted to distinct membrane compartments [J].
Abdul-Ghani, M ;
Gougeon, PY ;
Prosser, DC ;
Da-Silva, LF ;
Ngsee, JK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (09) :6225-6233
[2]   Neural localization of addicsin in mouse brain [J].
Akiduki, Saori ;
Ochiishi, Tomoyo ;
Ikemoto, Mitsushi J. .
NEUROSCIENCE LETTERS, 2007, 426 (03) :149-154
[3]   Approaches for extracting practical information from gene co-expression networks in plant biology [J].
Aoki, Koh ;
Ogata, Yoshiyuki ;
Shibata, Daisuke .
PLANT AND CELL PHYSIOLOGY, 2007, 48 (03) :381-390
[4]   Of weeds and men: what genomes teach us about plant cell biology [J].
Assaad, FF .
CURRENT OPINION IN PLANT BIOLOGY, 2001, 4 (06) :478-487
[5]   Unique features of the plant vacuolar sorting machinery [J].
Bassham, DC ;
Raikhel, NV .
CURRENT OPINION IN CELL BIOLOGY, 2000, 12 (04) :491-495
[6]   A Rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants [J].
Batoko, H ;
Zheng, HQ ;
Hawes, C ;
Moore, I .
PLANT CELL, 2000, 12 (11) :2201-2217
[7]  
Beeckman T., 1994, Plant Molecular Biology Reporter, V12, P37, DOI 10.1007/BF02668662
[8]  
BENHAMED M, 2008, PLANT J IN PRESS
[9]   THE GTPASE SUPERFAMILY - A CONSERVED SWITCH FOR DIVERSE CELL FUNCTIONS [J].
BOURNE, HR ;
SANDERS, DA ;
MCCORMICK, F .
NATURE, 1990, 348 (6297) :125-132
[10]   Membrane protein transport between the endoplasmic reticulum and the golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching [J].
Brandizzi, F ;
Snapp, EL ;
Roberts, AG ;
Lippincott-Schwartz, J ;
Hawes, C .
PLANT CELL, 2002, 14 (06) :1293-1309