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Altered phosphorylation and activation of pp60c-src during fibroblast mitosis

I Chackalaparampil1, D Shalloway

  • 1Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.

Cell
|March 25, 1988
PubMed

Insights

During mitosis, pp60c-src undergoes novel phosphorylation, enhancing its kinase activity 4-7 fold. This modification, independent of Tyr 416/527, suggests pp60c-src regulates mitosis-specific events.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • pp60c-src is a non-receptor tyrosine kinase involved in cell signaling.
  • Mitosis involves complex regulatory mechanisms controlling cell division.

Purpose of the Study:

  • To investigate the modifications and activity of pp60c-src during mitosis.
  • To determine if pp60c-src plays a role in mitosis-specific events.

Main Methods:

  • Utilized NIH 3T3 cells overexpressing c-src.
  • Analyzed pp60c-src phosphorylation sites (threonine, serine) during mitosis.
  • Assessed in vitro kinase activity and phosphopeptide analysis.
  • Employed electrophoretic mobility retardations for endogenous pp60c-src and pp60v-src.

Main Results:

  • Over half of pp60c-src is modified by threonine and serine phosphorylation in its amino-terminal region during mitosis.
  • Mitotic pp60c-src exhibits 4- to 7-fold enhanced in vitro kinase activity.
  • Modifications are independent of Tyr 416/Tyr 527 phosphorylation.
  • Endogenous pp60c-src and pp60v-src show similar modifications during mitosis.
  • Enhanced activity and modifications resolve near cell division.

Conclusions:

  • pp60c-src is subject to mitosis-specific regulation.
  • Enhanced pp60c-src kinase activity during mitosis suggests a role in regulating cell division events.
  • These findings highlight a potential link between pp60c-src signaling and mitotic progression.

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