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Gene Review

PIP2A  -  aquaporin PIP2-1

Arabidopsis thaliana

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High impact information on PIP2A

  • By contrast, the PIP2A plasma membrane protein was not mislocalized, and the secretion of Pi starvation-induced RNases was not affected in the mutant [1].
  • This report describes the cloning and expression of a new Arabidopsis PLD cDNA, designated PLDgamma, and the regulation of PLDgamma, -beta, and -alpha by phosphatidylinositol 4,5-bisphosphate (PIP2) and Ca2+ [2].
  • This binding ability correlates with the degree of conservation of a basic PIP2-binding motif located near the putative catalytic site [2].
  • The activity of the expressed PLDbeta is dependent on PIP2 and submicromolar amounts of Ca2+, inhibited by neomycin, and stimulated by a soluble factor from plant extracts [3].
  • The appearance of intracellular structures containing PIP1 and PIP2 homologs was occasionally observed after 2 h of salt treatment [4].

Biological context of PIP2A


Anatomical context of PIP2A

  • The role of plasma membrane aquaporins (PIPs) in water relations of Arabidopsis was studied by examining plants with reduced expression of PIP1 and PIP2 aquaporins, produced by crossing two different antisense lines [10].
  • Compared with controls, the double antisense (dAS) plants had reduced amounts of PIP1 and PIP2 aquaporins, and the osmotic hydraulic conductivity of isolated root and leaf protoplasts was reduced 5- to 30-fold [10].

Associations of PIP2A with chemical compounds

  • Thus the initiating methionine was acetylated or cleaved in native PIP1 and PIP2 isoforms respectively [9].


  1. PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 is a plant-specific SEC12-related protein that enables the endoplasmic reticulum exit of a high-affinity phosphate transporter in Arabidopsis. González, E., Solano, R., Rubio, V., Leyva, A., Paz-Ares, J. Plant Cell (2005) [Pubmed]
  2. Molecular heterogeneity of phospholipase D (PLD). Cloning of PLDgamma and regulation of plant PLDgamma, -beta, and -alpha by polyphosphoinositides and calcium. Qin, W., Pappan, K., Wang, X. J. Biol. Chem. (1997) [Pubmed]
  3. Molecular cloning and functional analysis of polyphosphoinositide-dependent phospholipase D, PLDbeta, from Arabidopsis. Pappan, K., Qin, W., Dyer, J.H., Zheng, L., Wang, X. J. Biol. Chem. (1997) [Pubmed]
  4. Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression. Boursiac, Y., Chen, S., Luu, D.T., Sorieul, M., van den Dries, N., Maurel, C. Plant Physiol. (2005) [Pubmed]
  5. A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots. Santoni, V., Vinh, J., Pflieger, D., Sommerer, N., Maurel, C. Biochem. J. (2003) [Pubmed]
  6. Immunochemical analysis of aquaporin isoforms in Arabidopsis suspension-cultured cells. Kobae, Y., Mizutani, M., Segami, S., Maeshima, M. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  7. Eight cDNA encoding putative aquaporins in Vitis hybrid Richter-110 and their differential expression. Baiges, I., Schäffner, A.R., Mas, A. J. Exp. Bot. (2001) [Pubmed]
  8. Specific plasma membrane aquaporins of the PIP1 subfamily are expressed in sieve elements and guard cells. Fraysse, L.C., Wells, B., McCann, M.C., Kjellbom, P. Biol. Cell (2005) [Pubmed]
  9. Methylation of aquaporins in plant plasma membrane. Santoni, V., Verdoucq, L., Sommerer, N., Vinh, J., Pflieger, D., Maurel, C. Biochem. J. (2006) [Pubmed]
  10. Plasma membrane aquaporins play a significant role during recovery from water deficit. Martre, P., Morillon, R., Barrieu, F., North, G.B., Nobel, P.S., Chrispeels, M.J. Plant Physiol. (2002) [Pubmed]
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