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Metabolic activation-related CD147-CD98 complex.

Daosong Xu¹, Martin E Hemler

¹Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Molecular & Cellular Proteomics : MCP

|May 20, 2005

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The CD147-CD98 cell surface supercomplex coordinates amino acid and lactate transport, impacting cell proliferation and energy metabolism. This study identifies a novel molecular complex crucial for cellular functions.

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Cell surface CD147 protein influences various cellular functions including proliferation and metabolism.
CD147 interacts with transporters and regulators, suggesting a role in complex cellular machinery.

Purpose of the Study:

To elucidate the specific transporter associations of CD147.
To investigate the role of CD147-associated complexes in cell proliferation and energy metabolism.

Main Methods:

Covalent cross-linking and mass spectrometry to identify protein associations.
Co-immunoprecipitation to confirm complex formation.
RNA interference (RNAi) knock-down experiments to assess functional impact.

Main Results:

Related Experiment Videos

CD147 selectively associates with CD98 heavy chain (CD98hc)-L-type amino acid transporter, ASCT2, and monocarboxylate transporters.
CD147 and CD98hc act as central organizers in these multicomponent cell surface complexes.
CD147 and CD98hc expression positively correlates with cell proliferation, and their reduction activates AMP-activated protein kinase, indicating metabolic disruption.

Conclusions:

A CD147-CD98 cell surface supercomplex plays a critical role in energy metabolism by coordinating lactate and amino acid transport.
The study demonstrates the utility of covalent cross-linking and mass spectrometry for identifying transmembrane protein complexes.
This methodology can be applied to study other transmembrane protein interactions.