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

被引：143

作者：

Temmei, Y

Uchida, S

Hoshino, D

Kanzawa, N

Kuwahara, M

Sasaki, S

Tsuchiya, T

机构：

[1] Sophia Univ, Fac Sci & Technol, Dept Chem, Chiyoda Ku, Tokyo 1028554, Japan

[2] Tokyo Med & Dent Univ, Grad Sch, Dept Nephrol, Tokyo 1138519, Japan

来源：

FEBS LETTERS | 2005年 / 579卷 / 20期

关键词：

aquaporin; direct interaction; plasma membrane intrinsic protein; phosphorylation; cAMP-dependent protein kinase A; Mimosa pudica;

D O I：

10.1016/j.febslet.2005.06.082

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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.

引用

页码：4417 / 4422

页数：6

共 40 条

[1]

Phosphorylation of plasma membrane aquaporin regulates temperature-dependent opening of tulip petals [J].