Proteomic Studies of the Intrinsically Unstructured Mammalian Proteome

Intrinsically unstructured proteins (IUPs) represent an important class of proteins primarily involved in cellular signaling and regulation. The aim of this study was to develop methodology for the enrichment and identification of IUPs. We show that heat treatment of NIH3T3 mouse fibroblast cell ext...

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Published inJournal of proteome research Vol. 5; no. 10; pp. 2839 - 2848
Main Authors Galea, Charles A, Pagala, Vishwajeeth R, Obenauer, John C, Park, Cheon-Gil, Slaughter, Clive A, Kriwacki, Richard W
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 01.10.2006
Subjects
Animals
Cell Nucleus - chemistry
Cytosol - chemistry
Electrophoresis, Gel, Two-Dimensional
Hot Temperature
Hydrophobic and Hydrophilic Interactions
Mice
NIH 3T3 Cells
Nuclear Proteins - analysis
Protein Conformation
Protein Denaturation
Proteins - analysis
Proteome - analysis
Proteomics - methods
Signal Transduction
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ISSN1535-3893
1535-3907
DOI10.1021/pr060328c

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Summary:Intrinsically unstructured proteins (IUPs) represent an important class of proteins primarily involved in cellular signaling and regulation. The aim of this study was to develop methodology for the enrichment and identification of IUPs. We show that heat treatment of NIH3T3 mouse fibroblast cell extracts at 98 °C selects for IUPs. The majority of these IUPs were cytosolic or nuclear proteins involved in cell signaling or regulation. These studies represent the first large-scale experimental investigation of the intrinsically unstructured mammalian proteome. Keywords: intrinsically unstructured proteins • disordered proteins • proteomics • mammalian proteome • heat denaturation
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ISSN:1535-3893
1535-3907
DOI:10.1021/pr060328c