Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 20, Pages 8328-8333Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0701103104
Keywords
bioinformatics; chemotaxis; phosphoproteomics; proteomics; cell migration
Categories
Funding
- NCI NIH HHS [R01 CA097022, CA097022] Funding Source: Medline
- NCRR NIH HHS [RR018522, P41 RR018522, P41 RR018522-04] Funding Source: Medline
- NIGMS NIH HHS [R01 GM068487, GM064346, U54 GM064346, GM068487] Funding Source: Medline
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Cell movement requires morphological polarization characterized by formation of a leading pseuclopodium (PD) at the front and a trailing rear at the back. However, little is known about how protein networks are spatially integrated to regulate this process at the system level. Here, we apply global proteome profiling in combination with newly developed quantitative phosphoproteomics approaches for comparative analysis of the cell body (CB) and PD proteome of chemotactic cells. The spatial relationship of 3,509 proteins and 228 distinct sites of phosphorylation were mapped revealing networks of signaling proteins that partition to the PD and/or the CB compartments. The major network represented in the PD includes integrin signaling, actin regulatory, and axon guidance proteins, whereas the CB consists of DNA/RNA metabolism, cell cycle regulation, and structural maintenance. Our findings provide insight into the spatial organization of signaling networks that control cell movement and provide a comprehensive system-wide profile of proteins and phosphorylation sites that control cell polarization.
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