MCP AbD Serotec
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/mcp.R300009-MCP200 on September 9, 2003.
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
R300009-MCP200v1
R300009-MCP200v2
R300009-MCP200v3
R300009-MCP200v5
2/11/1143    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yeung, Y.-G.
Right arrow Articles by Stanley, E. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yeung, Y.-G.
Right arrow Articles by Stanley, E. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Molecular & Cellular Proteomics 2:1143-1155, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

Review

Proteomic Approaches to the Analysis of Early Events in Colony-stimulating Factor-1 Signal Transduction*

Yee-Guide Yeung and E. Richard Stanley{ddagger}

From the Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461

The exposure of cells to growth factors leads to the rapid tyrosine phosphorylation of proteins that play critical roles in initiating cellular responses. These proteins are associated with other nontyrosine-phosphorylated proteins. Together, they represent less than 0.02% of the total cellular protein. To study their functions in growth factor signaling it is necessary to establish their identity, post-translational modifications, and interactions. We have focused on the characterization of this group of proteins during the early response of macrophages to the macrophage growth factor, colony-stimulating factor-1 (CSF-1). We review here the development of approaches to analysis of the rapid CSF-1-induced changes in the CSF-1 receptor tyrosine kinase and phosphotyrosyl signaling complexes. Recent advances in mass spectrometry technology are greatly facilitating the characterization of such complexes. These methods strongly support and enhance genetic approaches that are being used to analyze the function of individual signaling components and pathways.

{ddagger} To whom correspondence should be addressed: Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461. Tel.: 718-430-2344; Fax: 718-430-8567; E-mail: rstanley{at}aecom.yu.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
T. Wang, P. C. Hanington, M. Belosevic, and C. J. Secombes
Two Macrophage Colony-Stimulating Factor Genes Exist in Fish That Differ in Gene Organization and Are Differentially Expressed
J. Immunol., September 1, 2008; 181(5): 3310 - 3322.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Shah, K. Patel, S. Mukhopadhyay, F. Xu, G. Guo, and P. B. Sehgal
Membrane-associated STAT3 and PY-STAT3 in the Cytoplasm
J. Biol. Chem., March 17, 2006; 281(11): 7302 - 7308.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
V. Chitu, F. J. Pixley, F. Macaluso, D. R. Larson, J. Condeelis, Y.-G. Yeung, and E. R. Stanley
The PCH Family Member MAYP/PSTPIP2 Directly Regulates F-Actin Bundling and Enhances Filopodia Formation and Motility in Macrophages
Mol. Biol. Cell, June 1, 2005; 16(6): 2947 - 2959.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
F. J. Pixley, Y. Xiong, R. Y.-L. Yu, E. A. Sahai, E. R. Stanley, and B. H. Ye
BCL6 suppresses RhoA activity to alter macrophage morphology and motility
J. Cell Sci., May 1, 2005; 118(9): 1873 - 1883.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
A. Yamauchi, C. Kim, S. Li, C. C. Marchal, J. Towe, S. J. Atkinson, and M. C. Dinauer
Rac2-Deficient Murine Macrophages Have Selective Defects in Superoxide Production and Phagocytosis of Opsonized Particles
J. Immunol., November 15, 2004; 173(10): 5971 - 5979.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
X.-M. Dai, X.-H. Zong, V. Sylvestre, and E. R. Stanley
Incomplete restoration of colony-stimulating factor 1 (CSF-1) function in CSF-1-deficient Csf1op/Csf1op mice by transgenic expression of cell surface CSF-1
Blood, February 1, 2004; 103(3): 1114 - 1123.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.