Journal
FEBS LETTERS
Volume 579, Issue 20, Pages 4417-4422Publisher
WILEY
DOI: 10.1016/j.febslet.2005.06.082
Keywords
aquaporin; direct interaction; plasma membrane intrinsic protein; phosphorylation; cAMP-dependent protein kinase A; Mimosa pudica
Ask authors/readers for more resources
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;I is involved in regulation of the structure of the channel complex with MpMIP2;1 and thereby affects water channel activity. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available