4.6 Review

Scaffolds are 'active' regulators of signaling modules

Journal

FEBS JOURNAL
Volume 277, Issue 21, Pages 4376-4382

Publisher

WILEY
DOI: 10.1111/j.1742-4658.2010.07867.x

Keywords

cellular signaling; InaD; KSR1; MAPK module; phosphorylation of scaffold; protein kinase; PSD95; signaling cascade; signaling scaffold; Ste5

Funding

  1. Wellcome Trust [081665/Z/06/Z]
  2. European Community [205436]
  3. NKTH-OTKA [H07-A 74216]
  4. Wellcome Trust [081665/Z/06/Z] Funding Source: Wellcome Trust

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Signaling cascades, in addition to proteins with obvious signaling-relevant activities (e.g. protein kinases or receptors), also employ dedicated 'inactive' proteins whose functions appear to be the organization of the former components into higher order complexes through protein-protein interactions. The core function of signaling adaptors, anchors and scaffolds is the recruitment of proteins into one macromolecular complex. Several recent studies have demonstrated that the recruiter and the recruited molecules mutually influence each other in a scaffolded complex. This yields fundamentally novel properties for the signaling complex as a whole. Because these are not merely additive to the properties of the individual components, scaffolded signaling complexes may behave as functionally distinct modules.

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