Pseudoscaffolds and anchoring proteins: the difference is in the details

Biochem Soc Trans. 2017 Apr 15;45(2):371-379. doi: 10.1042/BST20160329.

Abstract

Pseudokinases and pseudophosphatases possess the ability to bind substrates without catalyzing their modification, thereby providing a mechanism to recruit potential phosphotargets away from active enzymes. Since many of these pseudoenzymes possess other characteristics such as localization signals, separate catalytic sites, and protein-protein interaction domains, they have the capacity to influence signaling dynamics in local environments. In a similar manner, the targeting of signaling enzymes to subcellular locations by A-kinase-anchoring proteins (AKAPs) allows for precise and local control of second messenger signaling events. Here, we will discuss how pseudoenzymes form 'pseudoscaffolds' and compare and contrast this compartment-specific regulatory role with the signal organization properties of AKAPs. The mitochondria will be the focus of this review, as they are dynamic organelles that influence a broad range of cellular processes such as metabolism, ATP synthesis, and apoptosis.

Keywords: A-kinase-anchoring protein; mitochondria; pseudoscaffold.

Publication types

  • Review
  • Research Support, U.S. Gov't, P.H.S.
  • Research Support, N.I.H., Extramural

MeSH terms

  • A Kinase Anchor Proteins / metabolism*
  • Animals
  • Cyclic AMP / metabolism
  • Humans
  • Mitochondria / enzymology*
  • Phosphoric Monoester Hydrolases / metabolism*
  • Phosphotransferases / metabolism*
  • Protein Interaction Domains and Motifs
  • Second Messenger Systems

Substances

  • A Kinase Anchor Proteins
  • Cyclic AMP
  • Phosphotransferases
  • Phosphoric Monoester Hydrolases