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 extracts at 98 degrees 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.
Galea
Charles A
CA
Department of Structural Biology, St. Jude Children's Research Hospital, and Department of Molecular Sciences, University of Tennessee Health Sciences Center, Memphis, Tennessee 38163, USA.
Pagala
Vishwajeeth R
VR
Obenauer
John C
JC
Park
Cheon-Gil
CG
Slaughter
Clive A
CA
Kriwacki
Richard W
RW
D000818:Animals; D002467:Cell Nucleus / Q000737:chemistry; D003600:Cytosol / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D051379:Mice; D041681:NIH 3T3 Cells; D009687:Nuclear Proteins / Q000032:analysis; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis*; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods*; D015398:Signal Transduction
D009687:Nuclear Proteins; D011506:Proteins; D020543:Proteome