UPF1-like helicases play roles in telomeric heterochromatin formation and X-chromosome inactivation and we focus here on variant surface glycoprotein (VSG) exclusion-factor-2 (VEX2), a UPF1-related protein in the African trypanosome. This bloodstream parasite evades host immunity by employing monogenic and switchable VSG expression, a form of antigenic variation which involves transcription of one telomeric VSG gene at a time. A trans-splicing compartment and the single VSG transcription factory are juxtaposed and enriched for VEX1 and VEX2, respectively, but our understanding of the VSG exclusion mechanism remains otherwise incomplete. Here, we sought VEX2-interacting partners, using cryomilling and affinity purification followed my LC-MS/MS analysis. We confirmed previous observations that VEX2 interacts with VEX1 and CAF-1, but also found evidence for weaker interactions and/or spatial proximity to telomere binding proteins.