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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Temmei Y,Uchida S,Hoshino D,Kanzawa N,Kuwahara M,Sasaki S,Tsuchiya T

doi

10.1016/j.febslet.2005.06.082

keywords:

subject

Has Abstract

pub_date

2005-08-15 00:00:00

pages

4417-22

issue

20

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00847-1

journal_volume

579

pub_type

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