Heregulin, a new interactor of the telosome/shelterin complex in human telomeres

Oncotarget
Javier A MenendezRuth Lupu

Abstract

Telomere length, shape and function depend on a complex of six core telomere-associated proteins referred to as the telosome or shelterin complex. We here demonstrate that the isoform β2 of the heregulin family of growth factors (HRGβ2) is a novel interactor of the telosome/shelterin complex in human telomeres. Analysis of protein-protein interactions using a high-throughput yeast two-hybrid (Y2H) screen identified RAP1, the only telomere protein that is conserved from yeasts to mammals, as a novel interacting partner of HRGβ2. Deletion analysis of RAP1 revealed that the linker domain, a region previously suggested to recruit negative regulators of telomere length, interacts specifically with HRGβ2. Co-immunoprecipitation and imaging experiments demonstrated that, in addition to RAP1, HRGβ2 could associate with the RAP1-associated telomeric repeat binding factor 2 (TRF2). Deletion analysis of HRGβ2 confirmed that a putative nuclear localization signal (NLS) was necessary for nuclear HRGβ2 to exert a negative regulation of telomere length whereas the N-terminus (extracellular) amino acids of HRGβ2 were sufficient to interact with RAP1/TRF2 and promote telomere shortening. Taken together, our studies identify nuclear HRGβ2 as one...Continue Reading

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Citations

Feb 20, 2020·Parasitology Research·Xianhe LiXichen Zhang
Feb 13, 2019·International Journal of Molecular Sciences·Sergey S ShishkinKsenia Lisitskaya
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Methods Mentioned

BETA
two-hybrid
Y2H
nuclear translocation
fluorescence microscopy
co-immunoprecipitation
immunoprecipitation
flow cytometry
PCR
transfection
electrophoresis

Software Mentioned

- QuaNT
Image
Cell Quest

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