A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots

被引:113
作者
Santoni, V
Vinh, J
Pflieger, D
Sommerer, N
Maurel, C
机构
[1] INRA, CNRS, Biochim & Physiol Mol Plantes Agro M, UM UMR 5004, F-34060 Montpellier, France
[2] Ecole Super Phys & Chim Ind Ville Paris, Neurobiol Lab, CNRS UMR 7637, F-75231 Paris 05, France
关键词
aquaporin; mass spectrometry (MS); phosphorylation; plasma membrane; root; two-dimensional electrophoresis;
D O I
10.1042/BJ20030159
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
Aquaporins are channel proteins that facilitate the diffusion of water across cell membranes. The genome of Arabidopsis thaliana encodes 35 full-length aquaporin homologues. Thirteen of them belong to the plasma membrane intrinsic protein (PIP) subfamily and predominantly sit at the plasma membrane (PM). In the present work we combine separations of membrane proteins (by one- and two-dimensional gel electrophoresis) with identification by MS (matrix-assisted laser-desorption ionization-time-of-flight and electrospray-ionization tandem MS) to take an inventory of aquaporin isoforms expressed in the PM of Arabidopsis thaliana roots. Our analysis provides direct evidence for the expression of five PIPs (PIP1; 1, PIP1;5, PIP2;1, PIP2;2 and PIP2;7) in the root PM and suggests the presence of at least three other PIP isoforms. In addition, we show that the same PIP isoform can be present under several forms with distinct isoelectric points. More specifically, we identify phosphorylated aquaporins in the PIP1 and PIP2 subgroups and suggest the existence of other post-translational modifications. Their identification should provide clues to reveal novel molecular mechanisms for aquaporin regulation.
引用
收藏
页码:289 / 296
页数:8
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