Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells

Yunhao Chen, Teck-Yew Low, Lee-Yee Choong, Rajarshi Sankar Ray, Yee-Ling Tan, Weiyi Toy, Qingsong Lin, Boon Keong Ang, Chee Hong Wong, Simin Lim, Bin Li, Choy-Leong Hew, Newman Siu-Kwan Sze, Brian J Druker, Yoon-Pin Lim

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2007-Jul
OriginalsprogEngelsk
TidsskriftProteomics
Vol/bind7
Udgave nummer14
Sider (fra-til)2384-2397
Antal sider13
ISSN1615-9853
DOI
StatusUdgivet - 1. jul. 2007

Fingeraftryk

Phosphorylation
Epidermal Growth Factor
Tyrosine
Cells
Epidermal Growth Factor Receptor
Neoplasms
Phosphotyrosine
Human Genome Project
Proteins
Proteome
gefitinib
Uterine Cervical Neoplasms
Genes
Modulation
Lipids
Substrates

Citer dette

Chen, Yunhao ; Low, Teck-Yew ; Choong, Lee-Yee ; Ray, Rajarshi Sankar ; Tan, Yee-Ling ; Toy, Weiyi ; Lin, Qingsong ; Ang, Boon Keong ; Wong, Chee Hong ; Lim, Simin ; Li, Bin ; Hew, Choy-Leong ; Sze, Newman Siu-Kwan ; Druker, Brian J ; Lim, Yoon-Pin. / Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells. I: Proteomics. 2007 ; Bind 7, Nr. 14. s. 2384-2397.
@article{aa8c3e60fc3b11dc86ef000ea68e967b,
title = "Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells",
abstract = "With the completion of the human genome project, analysis of enriched phosphotyrosyl proteins from epidermal growth factor (EGF)-induced phosphotyrosine proteome permits the identification of novel downstream substrates of the EGF receptor (EGFR). Using cICAT-based LC-MS/MS method, we identified and relatively quantified the tyrosine phosphorylation levels of 21 proteins between control and EGF-treated A431 human cervical cancer cells. Of these, Endofin, DCBLD2, and KIAA0582 were validated to be novel tyrosine-phosphorylation targets of EGF signaling and Iressa, a highly selective inhibitor of EGFR. In addition, EGFR activity was shown to be necessary for EGF-induced localization of Endofin, an FYVE domain-containing protein regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Although several groups have conducted phosphoproteomics of EGF signaling in recent years, our study is the first to identify and validate Endofin, DCBLD2, and KIAA0582 as part of a complex EGF phosphotyrosine signaling network. These novel data will provide new insights into the complex EGF signaling and may have implications on target-directed cancer therapeutics.",
keywords = "Amino Acid Sequence, Cell Line, Tumor, Epidermal Growth Factor, Humans, Intracellular Signaling Peptides and Proteins, Membrane Proteins, Molecular Sequence Data, Neoplasms, Phosphoproteins, Phosphotyrosine, Proteomics, Quinazolines, Serine Endopeptidases, Signal Transduction, Tandem Mass Spectrometry",
author = "Yunhao Chen and Teck-Yew Low and Lee-Yee Choong and Ray, {Rajarshi Sankar} and Yee-Ling Tan and Weiyi Toy and Qingsong Lin and Ang, {Boon Keong} and Wong, {Chee Hong} and Simin Lim and Bin Li and Choy-Leong Hew and Sze, {Newman Siu-Kwan} and Druker, {Brian J} and Yoon-Pin Lim",
year = "2007",
month = "7",
day = "1",
doi = "10.1002/pmic.200600968",
language = "English",
volume = "7",
pages = "2384--2397",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "14",

}

Chen, Y, Low, T-Y, Choong, L-Y, Ray, RS, Tan, Y-L, Toy, W, Lin, Q, Ang, BK, Wong, CH, Lim, S, Li, B, Hew, C-L, Sze, NS-K, Druker, BJ & Lim, Y-P 2007, 'Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells', Proteomics, bind 7, nr. 14, s. 2384-2397. https://doi.org/10.1002/pmic.200600968

Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells. / Chen, Yunhao; Low, Teck-Yew; Choong, Lee-Yee; Ray, Rajarshi Sankar; Tan, Yee-Ling; Toy, Weiyi; Lin, Qingsong; Ang, Boon Keong; Wong, Chee Hong; Lim, Simin; Li, Bin; Hew, Choy-Leong; Sze, Newman Siu-Kwan; Druker, Brian J; Lim, Yoon-Pin.

I: Proteomics, Bind 7, Nr. 14, 01.07.2007, s. 2384-2397.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Phosphoproteomics identified Endofin, DCBLD2, and KIAA0582 as novel tyrosine phosphorylation targets of EGF signaling and Iressa in human cancer cells

AU - Chen, Yunhao

AU - Low, Teck-Yew

AU - Choong, Lee-Yee

AU - Ray, Rajarshi Sankar

AU - Tan, Yee-Ling

AU - Toy, Weiyi

AU - Lin, Qingsong

AU - Ang, Boon Keong

AU - Wong, Chee Hong

AU - Lim, Simin

AU - Li, Bin

AU - Hew, Choy-Leong

AU - Sze, Newman Siu-Kwan

AU - Druker, Brian J

AU - Lim, Yoon-Pin

PY - 2007/7/1

Y1 - 2007/7/1

N2 - With the completion of the human genome project, analysis of enriched phosphotyrosyl proteins from epidermal growth factor (EGF)-induced phosphotyrosine proteome permits the identification of novel downstream substrates of the EGF receptor (EGFR). Using cICAT-based LC-MS/MS method, we identified and relatively quantified the tyrosine phosphorylation levels of 21 proteins between control and EGF-treated A431 human cervical cancer cells. Of these, Endofin, DCBLD2, and KIAA0582 were validated to be novel tyrosine-phosphorylation targets of EGF signaling and Iressa, a highly selective inhibitor of EGFR. In addition, EGFR activity was shown to be necessary for EGF-induced localization of Endofin, an FYVE domain-containing protein regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Although several groups have conducted phosphoproteomics of EGF signaling in recent years, our study is the first to identify and validate Endofin, DCBLD2, and KIAA0582 as part of a complex EGF phosphotyrosine signaling network. These novel data will provide new insights into the complex EGF signaling and may have implications on target-directed cancer therapeutics.

AB - With the completion of the human genome project, analysis of enriched phosphotyrosyl proteins from epidermal growth factor (EGF)-induced phosphotyrosine proteome permits the identification of novel downstream substrates of the EGF receptor (EGFR). Using cICAT-based LC-MS/MS method, we identified and relatively quantified the tyrosine phosphorylation levels of 21 proteins between control and EGF-treated A431 human cervical cancer cells. Of these, Endofin, DCBLD2, and KIAA0582 were validated to be novel tyrosine-phosphorylation targets of EGF signaling and Iressa, a highly selective inhibitor of EGFR. In addition, EGFR activity was shown to be necessary for EGF-induced localization of Endofin, an FYVE domain-containing protein regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Although several groups have conducted phosphoproteomics of EGF signaling in recent years, our study is the first to identify and validate Endofin, DCBLD2, and KIAA0582 as part of a complex EGF phosphotyrosine signaling network. These novel data will provide new insights into the complex EGF signaling and may have implications on target-directed cancer therapeutics.

KW - Amino Acid Sequence

KW - Cell Line, Tumor

KW - Epidermal Growth Factor

KW - Humans

KW - Intracellular Signaling Peptides and Proteins

KW - Membrane Proteins

KW - Molecular Sequence Data

KW - Neoplasms

KW - Phosphoproteins

KW - Phosphotyrosine

KW - Proteomics

KW - Quinazolines

KW - Serine Endopeptidases

KW - Signal Transduction

KW - Tandem Mass Spectrometry

U2 - 10.1002/pmic.200600968

DO - 10.1002/pmic.200600968

M3 - Journal article

VL - 7

SP - 2384

EP - 2397

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 14

ER -