Phosphorylation-dependent binding of 14-3-3 to Par3β, a human Par3-related cell polarity protein

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

Mammalian Par3α and Par3β/Par3L participate in cell polarity establishment and localize to tight junctions of epithelial cells; Par3α acts via binding to atypical PKC (aPKC). Here we show that Par3β as well as Par3α interacts with 14-3-3 proteins in a phosphorylation-dependent manner. In the interaction, Ser-746 of Par3β and the corresponding residue of Par3α (Ser-814) likely play a crucial role, since replacement of these residues by unphosphorylatable alanine results in a loss of interacting activity. The mutant Par3 proteins with the replacement are correctly recruited to tight junctions of MDCK cells and to membrane ruffles induced by an active form of the small GTPase Rac in HeLa cells. Thus, the interaction with 14-3-3 appears to be dispensable to Par3 localization. Consistent with this, the Par3α-14-3-3 interaction does not inhibit the Par3α-aPKC association required for the Par3α localization, although the aPKC-binding site lies close to the Ser-814-containing, 14-3-3-interacting region.

元の言語英語
ページ(範囲)211-218
ページ数8
ジャーナルBiochemical and Biophysical Research Communications
329
発行部数1
DOI
出版物ステータス出版済み - 4 1 2005

Fingerprint

14-3-3 Proteins
Phosphorylation
Monomeric GTP-Binding Proteins
Tight Junctions
Alanine
Binding Sites
Association reactions
Membranes
Cell Polarity
Madin Darby Canine Kidney Cells
Mutant Proteins
HeLa Cells
Proteins
Epithelial Cells
Cell Membrane
human PARD3 protein

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

@article{9360df5799494e54888dfdc9e22dbe5f,
title = "Phosphorylation-dependent binding of 14-3-3 to Par3β, a human Par3-related cell polarity protein",
abstract = "Mammalian Par3α and Par3β/Par3L participate in cell polarity establishment and localize to tight junctions of epithelial cells; Par3α acts via binding to atypical PKC (aPKC). Here we show that Par3β as well as Par3α interacts with 14-3-3 proteins in a phosphorylation-dependent manner. In the interaction, Ser-746 of Par3β and the corresponding residue of Par3α (Ser-814) likely play a crucial role, since replacement of these residues by unphosphorylatable alanine results in a loss of interacting activity. The mutant Par3 proteins with the replacement are correctly recruited to tight junctions of MDCK cells and to membrane ruffles induced by an active form of the small GTPase Rac in HeLa cells. Thus, the interaction with 14-3-3 appears to be dispensable to Par3 localization. Consistent with this, the Par3α-14-3-3 interaction does not inhibit the Par3α-aPKC association required for the Par3α localization, although the aPKC-binding site lies close to the Ser-814-containing, 14-3-3-interacting region.",
author = "Tomoko Izaki and Sachiko Kamakura and Motoyuki Kohjima and Hideki Sumimoto",
year = "2005",
month = "4",
day = "1",
doi = "10.1016/j.bbrc.2005.01.115",
language = "English",
volume = "329",
pages = "211--218",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Phosphorylation-dependent binding of 14-3-3 to Par3β, a human Par3-related cell polarity protein

AU - Izaki, Tomoko

AU - Kamakura, Sachiko

AU - Kohjima, Motoyuki

AU - Sumimoto, Hideki

PY - 2005/4/1

Y1 - 2005/4/1

N2 - Mammalian Par3α and Par3β/Par3L participate in cell polarity establishment and localize to tight junctions of epithelial cells; Par3α acts via binding to atypical PKC (aPKC). Here we show that Par3β as well as Par3α interacts with 14-3-3 proteins in a phosphorylation-dependent manner. In the interaction, Ser-746 of Par3β and the corresponding residue of Par3α (Ser-814) likely play a crucial role, since replacement of these residues by unphosphorylatable alanine results in a loss of interacting activity. The mutant Par3 proteins with the replacement are correctly recruited to tight junctions of MDCK cells and to membrane ruffles induced by an active form of the small GTPase Rac in HeLa cells. Thus, the interaction with 14-3-3 appears to be dispensable to Par3 localization. Consistent with this, the Par3α-14-3-3 interaction does not inhibit the Par3α-aPKC association required for the Par3α localization, although the aPKC-binding site lies close to the Ser-814-containing, 14-3-3-interacting region.

AB - Mammalian Par3α and Par3β/Par3L participate in cell polarity establishment and localize to tight junctions of epithelial cells; Par3α acts via binding to atypical PKC (aPKC). Here we show that Par3β as well as Par3α interacts with 14-3-3 proteins in a phosphorylation-dependent manner. In the interaction, Ser-746 of Par3β and the corresponding residue of Par3α (Ser-814) likely play a crucial role, since replacement of these residues by unphosphorylatable alanine results in a loss of interacting activity. The mutant Par3 proteins with the replacement are correctly recruited to tight junctions of MDCK cells and to membrane ruffles induced by an active form of the small GTPase Rac in HeLa cells. Thus, the interaction with 14-3-3 appears to be dispensable to Par3 localization. Consistent with this, the Par3α-14-3-3 interaction does not inhibit the Par3α-aPKC association required for the Par3α localization, although the aPKC-binding site lies close to the Ser-814-containing, 14-3-3-interacting region.

UR - http://www.scopus.com/inward/record.url?scp=13844280436&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=13844280436&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2005.01.115

DO - 10.1016/j.bbrc.2005.01.115

M3 - Article

VL - 329

SP - 211

EP - 218

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -