title: Novel candidate substrates of AMP-activated protein kinase identified in red blood cell lysates.
abstract: AMPK is a metabolic stress-sensing kinase with important functions for red blood cell (RBC) survival. By using a proteomic approach, we identified putative AMPK targets in hemoglobin-depleted lysates of RBC, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response. These data tie in with the phenotypic observations of AMPKalpha1-deficient RBC and provide reference for future studies.
authors.affiliation: Institute of Cell Biology, ETH Zurich, Zurich, Switzerland. ramon.thali@cell.biol.ethz.ch
authors.forename: Ramon F
authors.initials: RF
authors.lastname: Thali
authors.forename: Roland D
authors.initials: RD
authors.lastname: Tuerk
authors.forename: Roland
authors.initials: R
authors.lastname: Scholz
authors.forename: Yolanda
authors.initials: Y
authors.lastname: Yoho-Auchli
authors.forename: Rene A
authors.initials: RA
authors.lastname: Brunisholz
authors.forename: Dietbert
authors.initials: D
authors.lastname: Neumann
mesh_terms: D055372:AMP-Activated Protein Kinases / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D004789:Enzyme Activation; D004912:Erythrocytes / Q000201:enzymology*; D006454:Hemoglobins / Q000737:chemistry / Q000302:isolation & purification; D006801:Humans; D051379:Mice; D009532:Nickel / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D006454:Hemoglobins; D009532:Nickel; D055372:AMP-Activated Protein Kinases