Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation

cDNAs encoding aquaporins PIP1;1, PIP2;1, and TIP1;1 were isolated from Mimosa pudica (Mp) cDNA library. MpPIP1;1 exhibited no water channel activity; however, it facilitated the water channel activity of MpPIP2;1 in a phosphorylation-dependent manner. Mutagenesis analysis revealed that Ser-131 of M...

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Bibliographic Details
Published in:FEBS letters 2005-08, Vol.579 (20), p.4417-4422
Main Authors: Temmei, Yusuke, Uchida, Shinichi, Hoshino, Daisuke, Kanzawa, Nobuyuki, Kuwahara, Michio, Sasaki, Sei, Tsuchiya, Takahide
Format: Article
Language:English
Subjects:
Animals
AQP
Aquaporin
Aquaporins - genetics
Aquaporins - metabolism
cAMP-dependent protein kinase A
Cell Membrane - metabolism
Cyclic AMP-Dependent Protein Kinases - metabolism
Direct interaction
Gene Library
Immunoprecipitation
Membrane Proteins - genetics
Membrane Proteins - metabolism
Mimosa - genetics
Mimosa - metabolism
Mimosa pudica
Mutagenesis
Oocytes - metabolism
osmotic water permeability
Phosphorylation
PIP
PKA
Plant Proteins - genetics
Plant Proteins - metabolism
Plasma membrane intrinsic protein
TIP
tonoplast intrinsic protein
Xenopus
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Summary:cDNAs encoding aquaporins PIP1;1, PIP2;1, and TIP1;1 were isolated from Mimosa pudica (Mp) cDNA library. MpPIP1;1 exhibited no water channel activity; however, it facilitated the water channel activity of MpPIP2;1 in a phosphorylation-dependent manner. Mutagenesis analysis revealed that Ser-131 of MpPIP1;1 was phosphorylated by PKA and that cooperative regulation of the water channel activity of MpPIP2;1 was regulated by phosphorylation of Ser-131 of MpPIP1;1. Immunoprecipitation analysis revealed that MpPIP1;1 binds directly to MpPIP2;1 in a phosphorylation-independent manner, suggesting that phosphorylation of Ser-131 of MpPIP1;1 is involved in regulation of the structure of the channel complex with MpMIP2;1 and thereby affects water channel activity.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2005.06.082