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Dual-Specificity Protein Kinases

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Book cover Intracellular Signaling Mediators in the Circulatory and Ventilatory Systems

Abstract

Dual-specificity kinases (DSK; or Ser/Thr/Tyr kinases) phosphorylate their substrates on serine, threonine, and/or tyrosine residues. Dual-specificity kinases intervene in the regulation of cell growth, differentiation, and apoptosis. Dual-specificity kinases include, at least, members of the superfamily of mitogen-activated protein kinases as well as those of the family of glycogen synthase kinases.

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Notes

  1. 1.

    Protein Tau is a component of neurofibrillary tangles that is involved in Alzheimer’s disease. Six Tau isoforms exist in brain that differ by number of binding domains. Protein Tau interacts with tubulin to stabilize microtubules and promotes tubulin assembly into microtubules.

  2. 2.

    A.k.a. dimerization cofactor of hepatocyte nuclear factor HNF1α from muscle (DCoHM).

  3. 3.

    CDC-like kinase-1 is also called LAMMER, as it possesses a sequence of LAMMER motif.

  4. 4.

    Scottish: small. Kinase Wee1 was discovered in fission yeast Schizosaccharomyces pombe. Schizosaccharomyces pombe is a unicellular, rod-shaped organism used as a model organism in biology. Fission and budding yeasts (Saccharomyces cerevisiae) remains in phases G2 and G1 of the cell cycle for an extended period, respectively, as G2–M and G1–S transitions are tightly controlled, respectively.

  5. 5.

    Kinase PKMYT1 is also known as MYT1. However, the MYT1 alias is also used to designate myelin transcription factor-1 (MyT1 according to the rules defined in this book).

  6. 6.

    A.k.a. phosphatidyl ethanolamine-binding protein-2 (PEBP2).

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Thiriet, M. (2013). Dual-Specificity Protein Kinases. In: Intracellular Signaling Mediators in the Circulatory and Ventilatory Systems. Biomathematical and Biomechanical Modeling of the Circulatory and Ventilatory Systems, vol 4. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-4370-4_7

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