A Shared Docking Motif in TRF1 and TRF2 Used for Differential Recruitment of Telomeric Proteins

The binding of TRF1 and TRF2 to their shared binding partner TIN2 and other shelterin accessory factors takes place in two different ways. TRF1 binds to TIN2 through its TRF homology (TRFH) domain, which is also used for binding with shelterin-associated factor PinX1. The TIN2 binding site of TRF2 lies outside the TRFH domain. Instead, the TRFH domain functions as docking site for shelterin accessory factor Apollo. Interestingly, Apollo and the TRF1 TRFH domain do not interact.

Shelterin is a six-protein complex, protecting telomeres in mammalian cells. It contains the two closely related proteins TRF1 and TRF2, which recruit various proteins to the telomeres.

Related antibodies on antibodies-online.com:

TRF1

TRF2

TIN2

Apollon

PinX1

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