P38-Mediated phosphorylation of Eps15 endocytic adaptor protein

Yue Zhou; Tomohiro Tanaka; Naoyuki Sugiyama; Satoru Yokoyama; Yuki Kawasaki; Tsutomu Sakuma; Yasushi Ishihama; Ikuo Saiki; Hiroaki Sakurai

doi:10.1016/j.febslet.2013.11.020

P38-Mediated phosphorylation of Eps15 endocytic adaptor protein

Yue Zhou, Tomohiro Tanaka, Naoyuki Sugiyama, Satoru Yokoyama, Yuki Kawasaki, Tsutomu Sakuma, Yasushi Ishihama, Ikuo Saiki, Hiroaki Sakurai^*

^*Corresponding author for this work

Cancer Cell Biology

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Epidermal growth factor receptor pathway substrate 15 (Eps15) has been suggested to be involved in the endocytosis of cell surface receptors, including epidermal growth factor receptor (EGFR). Eps15 is phosphorylated at Tyr-849 upon stimulation with EGF during endocytic processes. In the present study, we found that stimulation of HeLa cells with EGF or TNF-α induced transient phosphorylation of Eps15 at Ser-796. Inhibition of p38 completely blocked phosphorylation and recombinant p38α directly phosphorylated the residue. These results demonstrate a novel stress kinase-mediated signaling pathway to Eps15 endocytic adapter protein.

Original language	English
Pages (from-to)	131-137
Number of pages	7
Journal	FEBS Letters
Volume	588
Issue number	1
DOIs	https://doi.org/10.1016/j.febslet.2013.11.020
State	Published - 2014/01/03

Keywords

EGF
Eps15
TAK1
TNF-α
p38

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2013.11.020

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title = "P38-Mediated phosphorylation of Eps15 endocytic adaptor protein",

abstract = "Epidermal growth factor receptor pathway substrate 15 (Eps15) has been suggested to be involved in the endocytosis of cell surface receptors, including epidermal growth factor receptor (EGFR). Eps15 is phosphorylated at Tyr-849 upon stimulation with EGF during endocytic processes. In the present study, we found that stimulation of HeLa cells with EGF or TNF-α induced transient phosphorylation of Eps15 at Ser-796. Inhibition of p38 completely blocked phosphorylation and recombinant p38α directly phosphorylated the residue. These results demonstrate a novel stress kinase-mediated signaling pathway to Eps15 endocytic adapter protein.",

keywords = "EGF, Eps15, TAK1, TNF-α, p38",

author = "Yue Zhou and Tomohiro Tanaka and Naoyuki Sugiyama and Satoru Yokoyama and Yuki Kawasaki and Tsutomu Sakuma and Yasushi Ishihama and Ikuo Saiki and Hiroaki Sakurai",

note = "Funding Information: We are grateful to Drs. Alexandre Benmerah (INSERM U1016, Institut Cochin, Paris, France) and Pier Paolo Di Fiore (IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy) for providing GFP-Eps15 expression plasmids and triple knocked-down HeLa cells, respectively. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas and Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology, Japan , and a Grant-in-Aid for the Cooperative Research Project from the Institute of Natural Medicine , University of Toyama in 2011. ",

year = "2014",

month = jan,

day = "3",

doi = "10.1016/j.febslet.2013.11.020",

language = "英語",

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pages = "131--137",

journal = "FEBS Letters",

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T1 - P38-Mediated phosphorylation of Eps15 endocytic adaptor protein

AU - Zhou, Yue

AU - Tanaka, Tomohiro

AU - Sugiyama, Naoyuki

AU - Yokoyama, Satoru

AU - Kawasaki, Yuki

AU - Sakuma, Tsutomu

AU - Ishihama, Yasushi

AU - Saiki, Ikuo

AU - Sakurai, Hiroaki

N1 - Funding Information: We are grateful to Drs. Alexandre Benmerah (INSERM U1016, Institut Cochin, Paris, France) and Pier Paolo Di Fiore (IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy) for providing GFP-Eps15 expression plasmids and triple knocked-down HeLa cells, respectively. This work was supported in part by Grants-in-Aid for Scientific Research on Innovative Areas and Scientific Research (C) from the Ministry of Education, Culture, Sports, Science and Technology, Japan , and a Grant-in-Aid for the Cooperative Research Project from the Institute of Natural Medicine , University of Toyama in 2011.

PY - 2014/1/3

Y1 - 2014/1/3

N2 - Epidermal growth factor receptor pathway substrate 15 (Eps15) has been suggested to be involved in the endocytosis of cell surface receptors, including epidermal growth factor receptor (EGFR). Eps15 is phosphorylated at Tyr-849 upon stimulation with EGF during endocytic processes. In the present study, we found that stimulation of HeLa cells with EGF or TNF-α induced transient phosphorylation of Eps15 at Ser-796. Inhibition of p38 completely blocked phosphorylation and recombinant p38α directly phosphorylated the residue. These results demonstrate a novel stress kinase-mediated signaling pathway to Eps15 endocytic adapter protein.

AB - Epidermal growth factor receptor pathway substrate 15 (Eps15) has been suggested to be involved in the endocytosis of cell surface receptors, including epidermal growth factor receptor (EGFR). Eps15 is phosphorylated at Tyr-849 upon stimulation with EGF during endocytic processes. In the present study, we found that stimulation of HeLa cells with EGF or TNF-α induced transient phosphorylation of Eps15 at Ser-796. Inhibition of p38 completely blocked phosphorylation and recombinant p38α directly phosphorylated the residue. These results demonstrate a novel stress kinase-mediated signaling pathway to Eps15 endocytic adapter protein.

KW - EGF

KW - Eps15

KW - TAK1

KW - TNF-α

KW - p38

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DO - 10.1016/j.febslet.2013.11.020

M3 - 学術論文

AN - SCOPUS:84890993987

SN - 0014-5793

VL - 588

SP - 131

EP - 137

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

P38-Mediated phosphorylation of Eps15 endocytic adaptor protein

Abstract

Keywords

ASJC Scopus subject areas

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