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PhosphoSerine/threonine binding domains: you can't pSERious?

M B Yaffe1, S J Smerdon

  • 1Center for Cancer Research, Massachusetts Institute of Technology, 77 Massachusetts Avenue, E18-580, Cambridge, MA 02139, USA. myaffe@mit.edu

Structure (London, England : 1993)
|April 5, 2001
PubMed
Summary

Protein phosphorylation is vital, with over 500 human kinase genes. Structural studies reveal how serine/threonine phosphorylation creates binding sites for signaling proteins, advancing our understanding of cellular processes.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Protein phosphorylation is a fundamental biological process regulating numerous cellular functions.
  • The human genome encodes over 500 protein kinase genes, highlighting its significance.
  • Phosphorylation events, particularly on serine, threonine, and tyrosine residues, are crucial for signal transduction.

Purpose of the Study:

  • To review structural insights into serine/threonine phosphorylation-dependent signal transduction.
  • To explore the role of phospho-amino acid binding proteins/modules in cellular signaling pathways.

Main Methods:

  • Review of existing structural data for proteins involved in serine/threonine phosphorylation.
  • Analysis of protein structures and their complexes to understand binding interactions.

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  • Integration of structural information with knowledge of signal transduction pathways.

    • Main Results:

    • Structural data reveals how phosphorylated serine and threonine residues form specific binding surfaces.
    • These surfaces facilitate the recognition and binding of specific phospho-amino acid binding proteins/modules.
    • The reviewed structures provide mechanistic insights into signal transduction mediated by serine/threonine phosphorylation.

    Conclusions:

    • Structural biology provides critical insights into the mechanisms of serine/threonine phosphorylation-dependent signaling.
    • Understanding these protein-protein interactions is key to deciphering complex cellular communication networks.
    • Further structural studies will continue to illuminate the intricate regulation of biological processes by phosphorylation.