Correlation Engine 2.0
Clear Search sequence regions


  • activity (1)
  • behavior (1)
  • cells (4)
  • chimera (1)
  • electron (3)
  • filaments (5)
  • glycolysis (2)
  • humans (1)
  • isoform (3)
  • liver (4)
  • muscle skeletal (1)
  • PFK1 (13)
  • PFKL (4)
  • PFKM (1)
  • pfkm protein, human (1)
  • plasma membrane (2)
  • platelet (2)
  • polymers (2)
  • protein human (1)
  • tetramer (2)
  • Sizes of these terms reflect their relevance to your search.

    Despite abundant knowledge of the regulation and biochemistry of glycolytic enzymes, we have limited understanding on how they are spatially organized in the cell. Emerging evidence indicates that nonglycolytic metabolic enzymes regulating diverse pathways can assemble into polymers. We now show tetramer- and substrate-dependent filament assembly by phosphofructokinase-1 (PFK1), which is considered the "gatekeeper" of glycolysis because it catalyzes the step committing glucose to breakdown. Recombinant liver PFK1 (PFKL) isoform, but not platelet PFK1 (PFKP) or muscle PFK1 (PFKM) isoforms, assembles into filaments. Negative-stain electron micrographs reveal that filaments are apolar and made of stacked tetramers oriented with exposed catalytic sites positioned along the edge of the polymer. Electron micrographs and biochemical data with a PFKL/PFKP chimera indicate that the PFKL regulatory domain mediates filament assembly. Quantified live-cell imaging shows dynamic properties of localized PFKL puncta that are enriched at the plasma membrane. These findings reveal a new behavior of a key glycolytic enzyme with insights on spatial organization and isoform-specific glucose metabolism in cells. © 2017 Webb et al.

    Citation

    Bradley A Webb, Anne M Dosey, Torsten Wittmann, Justin M Kollman, Diane L Barber. The glycolytic enzyme phosphofructokinase-1 assembles into filaments. The Journal of cell biology. 2017 Aug 07;216(8):2305-2313

    Expand section icon Mesh Tags

    Expand section icon Substances


    PMID: 28646105

    View Full Text