Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

Substrate Channeling

  • Anil Mehta
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_5550-2



The preferred local utilization within a protein complex of a locally synthesized substrate by shielding the nascent substrate from a molar excess of the same moiety in the surrounding bulk solution. The converse also occurs where that moiety is preferentially drained by an intracomplex “substrate steal” mechanism depriving the complex of essential substrate. The direction of the flux also depends on the accessibility of the relevant precursor pools. Membrane-linked multienzymes in the glycolysis pathway attached to red cell transporter proteins and the fatty acid synthase multienzyme assembly are key examples. Reference Mies et al. (2007) and its recent update from the same group (J Biol Chem in press) provide a good example.

The relationship to cancer follows a newly discovered example that utilizes a protein–protein shield that includes one isoform of the first metastatic suppressor ever to be discovered, nucleoside diphosphate...


Multiprotein Complex Nucleoside Diphosphate Kinase Substrate Channeling Complex Protein Kinase Unfetter Access 
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  1. Mies F, Spriet C, Héliot L, Sariban-Sohraby S (2007) Epithelial Na+ channel stimulation by n-3 fatty acids requires proximity to a membrane-bound A-kinase-anchoring protein complexed with protein kinase A and phosphodiesterase. J Biol Chem 282(25):18339–18347CrossRefPubMedGoogle Scholar
  2. Multiple Authors (2006) J Bioenerg Biomembr 38:149–270 (Special issue)Google Scholar
  3. Wieland T (2007) Interaction of nucleoside diphosphate kinase B with heterotrimeric G protein betagamma dimers: consequences on G protein activation and stability. Naunyn Schmiedebergs Arch Pharmacol 374(5–6):373–383CrossRefPubMedGoogle Scholar

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© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.Division of Cardiovascular MedicineUniversity of DundeeDundeeUK