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The regulation of the cell surface proteome by AMP‐activated protein kinase (604.5)
Author(s) -
Ross Eden,
Antonescu Costin
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.604.5
Subject(s) - microbiology and biotechnology , proteome , biotinylation , ampk , cell , protein kinase a , cell adhesion , endocytosis , chemistry , biology , amp activated protein kinase , proteomics , kinase , biochemistry , gene
The many proteins at the cell surface (collectively, the cell surface proteome) control numerous cellular functions. The amount of each protein at the cell surface is dynamically controlled by endocytosis and recycling. AMP‐activated protein kinase (AMPK) is an important metabolic regulator that responds to energetic stress, such as increased cellular AMP:ATP and certain hormones. Studies examining a small number of cell surface proteins suggest that AMPK may have an important role in regulating endomembrane traffic. How AMPK may more broadly regulate the cell surface proteome is not known. We have refined a method to isolate the cell surface proteome from cultured cells, involving biotinylation of surface‐exposed proteins in intact cells and purification of biotinylated proteins, which we coupled to quantitative mass spectrometry to identify novel AMPK‐regulated membrane traffic phenomena. We find that activation of AMPK results in a decrease in the cell surface abundance of the β1‐integrin, revealing a mechanism by which cellular metabolism may regulate cell adhesion and migration. Our results provide novel insight into the regulation of the cell surface proteome by metabolic stress signaling.