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Microtubule-associated protein 1A is the fibroblast HMW MAP undergoing mitogen-stimulated serine phosphorylation

A K Erickson1, L B Ray, T W Sturgill

  • 1Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.

Insights

Epidermal growth factor, serum, and insulin stimulate the phosphorylation of a specific microtubule-associated protein (MAP). This protein, identified as MAP1A, undergoes serine phosphorylation in response to these growth factors.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Microtubule-associated proteins (MAPs) play crucial roles in microtubule dynamics.
  • Growth factors and hormones are known regulators of cellular processes, including protein phosphorylation.

Purpose of the Study:

  • To investigate the effect of growth factors and hormones on microtubule-associated protein phosphorylation.
  • To identify the specific MAP involved and the nature of its modification.

Main Methods:

  • Utilized antibodies against microtubule-associated proteins (MAPs).
  • Employed immunoprecipitation with a monoclonal antibody to identify the phosphoprotein.
  • Analyzed phosphorylation on serine residues.

Main Results:

  • Phosphorylation of a 350 kDa MAP was stimulated 2-3 fold by epidermal growth factor or serum in fibroblasts.
  • Insulin stimulated the same phosphorylation in adipocytes.
  • Phosphorylation occurred on serine residues, peaking within 15-20 minutes.
  • The phosphoprotein was identified as MAP1A.

Conclusions:

  • MAP1A is a target for growth factor and insulin signaling pathways.
  • MAP1A phosphorylation is a rapid cellular response to specific extracellular stimuli.
  • This phosphorylation event involves serine residues and is cell-type specific depending on the stimulus.

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