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Partners in crime: POPX2 phosphatase and its interacting proteins in cancer

Pu Rum Kim1, Songjing Zhang1, Muhammad Bakhait Rahmat1

  • 1School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.

Cell Death & Disease
|October 10, 2020
PubMed

Insights

Protein phosphatases, like POPX2 (Partner of PIX 2), are crucial in cell signaling but less understood than kinases. This review explores POPX2

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Oncology

Background:

  • Protein phosphorylation and dephosphorylation are key to cell signaling and function.
  • Kinases and phosphatases regulate vital cellular processes, with phosphatases being less studied.
  • Phosphatases can target numerous substrates, complicating their functional analysis.

Purpose of the Study:

  • To review the binding partners of POPX2 (Partner of PIX 2), a serine/threonine phosphatase.
  • To explore the cellular functions of POPX2 through its protein-protein interaction network (interactome).
  • To focus on POPX2's role in cancer progression and metastasis.

Main Methods:

  • Literature review of studies on POPX2 and its interacting proteins.
  • Analysis of the known functions associated with POPX2's binding partners.
  • Synthesis of information regarding POPX2's impact on cancer cell motility and invasiveness.

Main Results:

  • POPX2 interacts with various proteins, influencing diverse cellular functions.
  • The phosphatase POPX2 has been implicated in cancer cell motility and invasiveness.
  • POPX2's role in metastasis is complex and stage-dependent, mediated by its substrates and interactors.

Conclusions:

  • Understanding POPX2's interactome is crucial for elucidating its biological roles.
  • POPX2 plays a significant, multifaceted role in cancer progression and metastasis.
  • Further research into POPX2 and its partners could reveal novel therapeutic targets for cancer.

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