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. 2015 Dec 14;291(7):3145–3157. doi: 10.1074/jbc.M115.703058

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© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Author's Choice—Final version free via Creative Commons CC-BY license.

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FIGURE 8. — The combined cysteine-rich (C) and stalk (S) region of ADAM10 without the disintegrin (D) is sufficient to interact with Tspan14. A, HEK-293T cells were mock transfected (−) or transfected with FLAG-tagged human CD9 or Tspan14, with co-transfection of Myc-tagged human ADAM10, or pDisplay constructs containing ADAM10DCS or ADAM10CS, which also possessed Myc tags. Cells were lysed in 1% digitonin lysis buffer and immunoprecipitated with an anti-FLAG antibody. Immunoprecipitated proteins were blotted with anti-Myc tag antibody (top panel) or anti-FLAG antibody (lower panel). Whole cell lysates were probed with the anti-Myc tag antibody (middle panel). B, data in panel A (upper panel) were quantitated from three experiments. Data were log transformed and compared statistically with a one-way ANOVA with a Dunnett's multiple comparison test against the mock. Tspan14 bound significantly to ADAM10DCS (p < 0.0001) and ADAM10CS (p < 0.0001). A diagrammatic representation of the ADAM10 constructs is shown below the graph. C, HEK-293T cells were mock transfected (−) or transfected with FLAG-tagged human CD9 or Tspan14, with co-transfection of pDisplay ADAM10CS or ADAM10S. Cells were treated as in panel A. D, data in panel C were quantitated from three experiments. Data were log transformed and compared statistically with a one-way ANOVA with a Dunnett's multiple comparison test against the mock. Tspan14 bound significantly to ADAM10CS (p < 0.0001) and ADAM10S (p < 0.001).