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Challenges in plasma membrane phosphoproteomics

  1. Author:
    Orsburn, B. C.
    Stockwin, L. H.
    Newton, D. L.

  2. Author Address

    [Orsburn, BC; Stockwin, LH; Newton, DL] NCI, Drug Mech Grp, Dev Therapeut Program, SAIC Frederick Inc, Frederick, MD 21702 USA.;Newton, DL (reprint author), NCI, Drug Mech Grp, Dev Therapeut Program, SAIC Frederick Inc, Frederick, MD 21702 USA;newtondianne@mail.nih.gov
    1. Year: 2011
    2. Date: Aug
  2. Journal: Expert Review of Proteomics
    1. 8
    2. 4
    3. Pages: 483-494
  4. Type of Article: Review
  5. ISSN: 1478-9450
  1. Abstract:

    The response to extracellular stimuli often alters the phosphorylation state of plasma membrane-associated proteins. In this regard, generation of a comprehensive membrane phosphoproteome can significantly enhance signal transduction and drug mechanism studies. However, analysis of this subproteome is regarded as technically challenging, given the low abundance and insolubility of integral membrane proteins, combined with difficulties in isolating, ionizing and fragmenting phosphopeptides. In this article, we highlight recent advances in membrane and phosphoprotein enrichment techniques resulting in improved identification of these elusive peptides. We also describe the use of alternative fragmentation techniques, and assess their current and future value to the field of membrane phosphoproteomics.

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External Sources

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  2. DOI: 10.1586/epr.11.40
  3. View record in Web of Science®
  4. WOS: 000294139500012

Library Notes

  1. Fiscal Year: FY2010-2011
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