The Phosphorylation of the Microtubule-Associated Tau Proteins

  • Jacques Baudier
  • R. David Cole
Part of the Advances in Behavioral Biology book series (ABBI, volume 34)

Abstract

Extracellular signals, including a variety of neurotransmitters and hormones produce diverse physiological responses in neurons but until recently, little was known about the molecular mechanims that underlie these responses. There is now considerable evidence indicating that protein phosphorylation plays an important role in neuronal responses to extracellular messengers (for review see 1). Protein phosphorylation is involved in a shuttle: i) the substrate protein is phosphorylated when a protein kinase transfers the terminal phosphate from ATP to the substrate protein; the addition of the charged phosphate group to the protein modulates its function, presumably by changing its conformation; ii) the phosphate group can be removed from the protein by a phosphatase restoring the protein to its original functional state. Such a shuttle is now evident in microtubule proteins. Microtubules are one of the major constituents of neuronal cytoskeletons and play important roles in regulating cell morphology, intracellular transport processes and secretions. The microtubules are polymers of tubulin and they also contain accessory proteins, notably MAP1, MAP2, and the tau proteins.2

Keywords

Electrophoresis MgCl Serine Polypeptide Tryptophan 

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Jacques Baudier
    • 1
  • R. David Cole
    • 1
  1. 1.Department of BiochemistryUniversity of CaliforniaBerkeleyUSA

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