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Purification and structural analyses of ABCG2.

Christopher A McDevitt1, Richard Collins, Ian D Kerr

  • 1Nuffield Department of Clinical Laboratory Sciences, John Radcliffe Hospital, University of Oxford, Oxford, OX3 9DU, United Kingdom.

Advanced Drug Delivery Reviews
|January 7, 2009
PubMed
Summary

The ATP-binding cassette transporter G2 (ABCG2) protein

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • ATP-binding cassette transporter G2 (ABCG2) is a multidrug transporter crucial for cancer cell resistance.
  • ABCG2 is also expressed in barrier tissues and hematopoietic stem cells, but its molecular mechanism is poorly understood.
  • Unlike other multidrug transporters (ABCB1, ABCC1), ABCG2's oligomeric state and function remain controversial.

Purpose of the Study:

  • To review and critically assess the oligomeric state of ABCG2.
  • To analyze low-resolution structural data and recent molecular models of ABCG2.
  • To discuss the challenges in elucidating ABCG2's molecular mechanism.

Main Methods:

  • Literature review focusing on biochemical studies and structural data.

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  • Critical assessment of molecular models based on bacterial ABC transporter structures.
  • Analysis of low-resolution structural findings related to ABCG2 oligomerization.

    • Main Results:

    • Biochemical studies present conflicting data regarding ABCG2's oligomeric state, suggesting higher-order oligomers beyond a homodimer.
    • Low-resolution structural data and molecular models offer insights but do not provide a definitive mechanism.
    • ABCG2's distinct topology contributes to the complexity of understanding its function.

    Conclusions:

    • The precise oligomeric assembly and molecular mechanism of ABCG2 remain elusive.
    • Further structural and biochemical investigations are needed to resolve the controversies surrounding ABCG2.
    • Understanding ABCG2's mechanism is critical due to its role in multidrug resistance and stem cell biology.