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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

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SOCS1: phosphorylation, dimerization and tumor suppression

Frédéric Lessard1, Emmanuelle Saint-Germain1, Lian Mignacca1

  • 1Département de Biochimie et Médecine Moléculaire, Université de Montréal, Montréal, Québec, Canada.

Oncoscience
|January 28, 2020
PubMed

Insights

Suppressor of cytokine signaling (SOCS) proteins inhibit JAK-STAT signaling and tumor suppression. Reactivating the SOCS1-p53 axis with dasatinib and PRIMA offers new cancer treatment strategies.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • Suppressor of cytokine signaling (SOCS) proteins regulate cell growth, differentiation, and apoptosis.
  • SOCS1 and SOCS3 are implicated in tumor suppression via interaction with p53.
  • SRC family kinases (SFK) phosphorylate SOCS1, inhibiting its tumor suppressor function.

Purpose of the Study:

  • To investigate the role of SFK in SOCS1 regulation.
  • To explore therapeutic strategies for reactivating the SOCS1-p53 tumor suppressor axis.

Main Methods:

  • Investigated SOCS1 phosphorylation by SFK.
  • Utilized SFK inhibitor dasatinib and p53 activator PRIMA.
  • Assessed reactivation of the SOCS1-p53 axis.

Main Results:

  • SRC family kinases phosphorylate SOCS1, inhibiting its interaction with p53.
  • Dasatinib in combination with PRIMA reactivated the SOCS1-p53 tumor suppressor axis.

Conclusions:

  • SFK activity disrupts SOCS1-mediated tumor suppression.
  • Targeting SFK and p53 presents a novel therapeutic approach for cancer treatment.
Keywords:
P53SH2 domainsSRC kinasescytokine singling

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