Heat shock-induced dissociation of TRF2 from telomeres does not initiate a telomere-dependent DNA damage response.
Telomeric repeat binding factor 2 (TRF2) is a well-studied shelterin complex subunit that plays a major role in the protection of chomosome ends and the prevention of the telomere-associated DNA damage response. We show that heat shock induces the dissociation of TRF2 from telomeres in human primary and cancer cell cultures. TRF2 is not simply degraded in response to heat shock, but redistributed thoughout the nucleoplasm. This TRF2 depletion/redistribution does not initiate the DNA damage response at chomosome termini.
Laboratory of Structural and Functional Organization of Chomosomes, Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia; Department of Molecular Biology, Lomonosov Moscow State University, Moscow, Russia.
Nadezhda V
NV
Petrova
Artem K
AK
Velichko
Omar L
OL
Kantidze
Sergey V
SV
Razin
D002460:Cell Line; D004249:DNA Damage / Q000502:physiology*; D005347:Fibroblasts / Q000378:metabolism; D006358:Hot Temperature / Q000009:adverse effects*; D006801:Humans; D061986:MCF-7 Cells; D016615:Telomere / Q000235:genetics / Q000378:metabolism*; D035341:Telomeric Repeat Binding Protein 2 / Q000378:metabolism*
C504753:TERF2 protein, human; D035341:Telomeric Repeat Binding Protein 2
53BP1; DNA damage response; TRF2; heat shock; heat shock response; telomeres; γH2AX