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Title: Profiling Signaling Polarity in Chemotactic Cells

Abstract

While directional movement requires morphological polarization characterized by formation of a leading pseudopodium at the front and a trailing rear at the back, little is known about how protein networks are spatially integrated to regulate this process. Here, we utilize a unique pseudopodial purification system and quantitative proteomics and phosphoproteomics to map the spatial relationship of 3509 proteins and 228 distinct sites of phosphorylation in polarized cells. Networks of signaling proteins, metabolic pathways, actin regulatory proteins, and kinase-substrate cascades were found to partition to different poles of the cell including components of the Ras/ERK pathway. Also, several novel proteins were found to be differentially phosphorylated at the front or rear of polarized cells and to localize to distinct subcellular structures. Our findings provide insight into the spatial organization of signaling networks that control cell movement and provide a comprehensive profile of proteins and their sites of phosphorylation that control cell polarization.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Org.:
USDOE
OSTI Identifier:
912509
Report Number(s):
PNNL-SA-51866
Journal ID: ISSN 0027-8424; PNASA6; 11391; 400412000; TRN: US200801%%1060
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America, 104(20):8328-8333; Journal Volume: 104; Journal Issue: 20
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ACTIN; BIOLOGICAL PATHWAYS; PHOSPHORYLATION; POLARIZATION; PROTEINS; PURIFICATION; Phosphoproteome, IMAC, stable isotope dual labeling, global proteome, cell metastasis, pseudopodia, cell signaling; Environmental Molecular Sciences Laboratory

Citation Formats

Wang, Yingchun, Ding, Shi-Jian, Wang, Wei, Jacobs, Jon M., Qian, Weijun, Moore, Ronald J., Yang, Feng, Camp, David G., Smith, Richard D., and Klemke, Richard L. Profiling Signaling Polarity in Chemotactic Cells. United States: N. p., 2007. Web. doi:10.1073/pnas.0701103104.
Wang, Yingchun, Ding, Shi-Jian, Wang, Wei, Jacobs, Jon M., Qian, Weijun, Moore, Ronald J., Yang, Feng, Camp, David G., Smith, Richard D., & Klemke, Richard L. Profiling Signaling Polarity in Chemotactic Cells. United States. doi:10.1073/pnas.0701103104.
Wang, Yingchun, Ding, Shi-Jian, Wang, Wei, Jacobs, Jon M., Qian, Weijun, Moore, Ronald J., Yang, Feng, Camp, David G., Smith, Richard D., and Klemke, Richard L. Tue . "Profiling Signaling Polarity in Chemotactic Cells". United States. doi:10.1073/pnas.0701103104.
@article{osti_912509,
title = {Profiling Signaling Polarity in Chemotactic Cells},
author = {Wang, Yingchun and Ding, Shi-Jian and Wang, Wei and Jacobs, Jon M. and Qian, Weijun and Moore, Ronald J. and Yang, Feng and Camp, David G. and Smith, Richard D. and Klemke, Richard L.},
abstractNote = {While directional movement requires morphological polarization characterized by formation of a leading pseudopodium at the front and a trailing rear at the back, little is known about how protein networks are spatially integrated to regulate this process. Here, we utilize a unique pseudopodial purification system and quantitative proteomics and phosphoproteomics to map the spatial relationship of 3509 proteins and 228 distinct sites of phosphorylation in polarized cells. Networks of signaling proteins, metabolic pathways, actin regulatory proteins, and kinase-substrate cascades were found to partition to different poles of the cell including components of the Ras/ERK pathway. Also, several novel proteins were found to be differentially phosphorylated at the front or rear of polarized cells and to localize to distinct subcellular structures. Our findings provide insight into the spatial organization of signaling networks that control cell movement and provide a comprehensive profile of proteins and their sites of phosphorylation that control cell polarization.},
doi = {10.1073/pnas.0701103104},
journal = {Proceedings of the National Academy of Sciences of the United States of America, 104(20):8328-8333},
number = 20,
volume = 104,
place = {United States},
year = {Tue May 15 00:00:00 EDT 2007},
month = {Tue May 15 00:00:00 EDT 2007}
}