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. 2015 Jun 4;96(6):955–961. doi: 10.1016/j.ajhg.2015.04.014

Figure 2.

Figure 2

Functional Characterization of the p.Val741Glu Substitution in GPR126

(A) Graphical representation of FLAG-tagged human GPR126 constructs corresponding to the wild-type (WT) protein, the p.Val741Glu substitution, a variant with disruption in the catalytic triad (p.His811Ala) that mediates autoproteolysis, and a deletion construct lacking the N-terminal fragment (ΔNT).

(B) Immunoblots of samples from transfected HEK293 cells show total cell lysate (left) or surface-labeled proteins (right). The control cells were transfected with the empty expression vector. The cleaved (filled arrowhead) and uncleaved full-length (open arrowhead) proteins are noted. The autoproteolytic activity of the p.Val741Glu construct was consistently reduced, but some cleaved product was evident on long exposures. The blot shown is representative of three independent experiments.