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HuR regulates telomerase activity through TERC methylation.

Hao Tang1,2, Hu Wang3,4, Xiaolei Cheng1

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The RNA-binding protein HuR promotes telomerase assembly by facilitating TERC methylation. Mutations disrupting HuR binding cause telomere shortening and bone marrow failure, linking HuR to telomere biology and related diseases.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Telomerase, composed of TERC and TERT, is crucial for maintaining telomere length.
  • Mutations in TERC are associated with human diseases, but the mechanisms remain unclear.

Purpose of the Study:

  • To investigate the role of RNA-binding protein HuR in telomerase assembly and TERC-associated diseases.
  • To elucidate the mechanism by which HuR influences TERC function and telomere maintenance.

Main Methods:

  • Co-immunoprecipitation assays to assess HuR-TERC association.
  • RNA methylation analysis to quantify TERC C106 methylation.
  • Telomerase activity assays and telomere length measurements.
  • Mouse hematopoietic stem cell renewal assays.

Main Results:

  • HuR directly binds to TERC and promotes its C106 methylation, facilitating TERC/TERT complex assembly.
  • Dyskeratosis congenita (DC)-associated TERC mutations (U100A, G107U, GC107/108AG) impair HuR binding and TERC methylation.
  • Reduced HuR binding and TERC methylation lead to decreased telomerase activity and telomere shortening.
  • HuR deficiency or disruption of HuR binding/methylation sites in TERC impairs mouse hematopoietic stem cell renewal, mimicking DC bone marrow failure.

Conclusions:

  • HuR plays a critical role in telomerase function by promoting TERC methylation and complex assembly.
  • Disruption of HuR-TERC interaction underlies telomere shortening and bone marrow failure in TERC-associated diseases like DC.
  • This study reveals a novel function of HuR in telomere maintenance and disease pathogenesis.