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Specific plasma membrane aquaporins of the PIP1 subfamily are expressed in sieve elements and guard cells

Fraysse, Laure LU ; Wells, Brian; McCann, Maureen C and Kjellbom, Per LU (2005) In Biology of the Cell 97(7). p.519-534
Abstract
Background information. Transmembrane water flow is aided by water-specific channel proteins, aquaporins. Plant genomes code for approx. 35 expressed and functional aquaporin isoforms. Plant aquaporins fall into four different subfamilies of which the PIPS (plasma membrane intrinsic proteins) constitute the largest and evolutionarily most conserved subfamily with 13 members in Arabidopsis and maize. Furthermore, the PIPs can be divided into two phylogenetic groups, PIP1 and PIP2, of which the PIP1 isoforms are most tightly conserved, sharing > 90% amino acid sequence identity. As the nomenclature implies, the majority of PIPs have been shown to be localized at the plasma membrane. Recently, two highly abundant plasma membrane... (More)
Background information. Transmembrane water flow is aided by water-specific channel proteins, aquaporins. Plant genomes code for approx. 35 expressed and functional aquaporin isoforms. Plant aquaporins fall into four different subfamilies of which the PIPS (plasma membrane intrinsic proteins) constitute the largest and evolutionarily most conserved subfamily with 13 members in Arabidopsis and maize. Furthermore, the PIPs can be divided into two phylogenetic groups, PIP1 and PIP2, of which the PIP1 isoforms are most tightly conserved, sharing > 90% amino acid sequence identity. As the nomenclature implies, the majority of PIPs have been shown to be localized at the plasma membrane. Recently, two highly abundant plasma membrane aquaporins, SoPIP2;1 and SoPIP1;2, have been purified and structurally characterized. Results. We report the cloning of a cDNA encoding SoPIP1;2 and show that there are at least five additional sequences homologous with SoPIP2;1 and SoPIP1;2 in the spinach genome. To understand their role in planta, we have investigated the cellular localization of the aquaporin homologues SoPIP1;2 and SoPIP1;1. By Western and Northern-blot analyses and by immunocytochemical detection at the light and electron microscopic levels, we show that SoPIP1;2 is highly expressed in phloem sieve elements of leaves, roots and petioles and that SoPIP1;1 is present in stomatal guard cells. Conclusions. Localization of the two abundant aquaporin isoforms suggests roles for specific PIPs of the PIP1 subgroup in phloem loading, transport and unloading, and in stomatal movements. (Less)
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Contribution to journal
publication status
published
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in
Biology of the Cell
volume
97
issue
7
pages
519 - 534
publisher
Portland Press
external identifiers
  • pmid:15898953
  • wos:000230780300004
  • scopus:21644480409
ISSN
0248-4900
language
English
LU publication?
yes
id
9c79feb5-5de1-4c62-b315-cea691b447b3 (old id 152480)
alternative location
http://www.biolcell.org/boc/097/boc0970519.htm
date added to LUP
2007-07-05 09:42:20
date last changed
2017-11-05 03:36:13
@article{9c79feb5-5de1-4c62-b315-cea691b447b3,
  abstract     = {Background information. Transmembrane water flow is aided by water-specific channel proteins, aquaporins. Plant genomes code for approx. 35 expressed and functional aquaporin isoforms. Plant aquaporins fall into four different subfamilies of which the PIPS (plasma membrane intrinsic proteins) constitute the largest and evolutionarily most conserved subfamily with 13 members in Arabidopsis and maize. Furthermore, the PIPs can be divided into two phylogenetic groups, PIP1 and PIP2, of which the PIP1 isoforms are most tightly conserved, sharing > 90% amino acid sequence identity. As the nomenclature implies, the majority of PIPs have been shown to be localized at the plasma membrane. Recently, two highly abundant plasma membrane aquaporins, SoPIP2;1 and SoPIP1;2, have been purified and structurally characterized. Results. We report the cloning of a cDNA encoding SoPIP1;2 and show that there are at least five additional sequences homologous with SoPIP2;1 and SoPIP1;2 in the spinach genome. To understand their role in planta, we have investigated the cellular localization of the aquaporin homologues SoPIP1;2 and SoPIP1;1. By Western and Northern-blot analyses and by immunocytochemical detection at the light and electron microscopic levels, we show that SoPIP1;2 is highly expressed in phloem sieve elements of leaves, roots and petioles and that SoPIP1;1 is present in stomatal guard cells. Conclusions. Localization of the two abundant aquaporin isoforms suggests roles for specific PIPs of the PIP1 subgroup in phloem loading, transport and unloading, and in stomatal movements.},
  author       = {Fraysse, Laure and Wells, Brian and McCann, Maureen C and Kjellbom, Per},
  issn         = {0248-4900},
  language     = {eng},
  number       = {7},
  pages        = {519--534},
  publisher    = {Portland Press},
  series       = {Biology of the Cell},
  title        = {Specific plasma membrane aquaporins of the PIP1 subfamily are expressed in sieve elements and guard cells},
  volume       = {97},
  year         = {2005},
}