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
N1 - Funding Information:
We are grateful to Miki Matsuo (Kyushu University), Yohko Kage (Kyushu University and JST), and Natsuko Yoshiura (Kyushu University) for technical assistance, and to Minako Nishino (Kyushu University and JST) for secretarial assistance. This work was supported in part by Grants-in-Aid for Scientific Research and National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and by CREST of JST (Japan Science and Technology Agency) and BIRD of JST.
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 - https://www.scopus.com/pages/publications/13844280436
UR - https://www.scopus.com/pages/publications/13844280436#tab=citedBy
U2 - 10.1016/j.bbrc.2005.01.115
DO - 10.1016/j.bbrc.2005.01.115
M3 - Article
C2 - 15721295
AN - SCOPUS:13844280436
SN - 0006-291X
VL - 329
SP - 211
EP - 218
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -