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. Author manuscript; available in PMC: 2009 Aug 4.
Published in final edited form as: FEBS Lett. 2007 Aug 14;581(23):4403–4410. doi: 10.1016/j.febslet.2007.08.008

Figure 3.

Figure 3

GRASP-1 serves as a scaffold protein for the JNK signaling pathway. (A) Mapping of the MEKK1- and JNK1-binding sites in GRASP-1. MEKK1- and JNK-interaction sites were mapped by coimmunoprecipitation studies using HEK293T cells co-transfected with either HA-MEKK1 or HA-JNK1 plus the indicated truncation or internal deletion mutants of GRASP-1. The D6 deletion abolished the interaction with JNK1. MEKK-1 appeared to interact with two sites in the C-terminal fragment and the interaction existed until both D6 and D12 were deleted. (B) GRASP-1 mutants deficient in JNK (Δ6) and/or MEKK1 binding (Δ6–Δ12) do not activate JNK. Western analysis was performed with anti-phospho-Jun antibody on lysates from HEK293T cells transfected with empty vector pRK5, GRASP1-N, GRASP1-C, GRASP1-CΔ6 or GRASP1-CΔ6–Δ12. Nocodazole-treatment on cells transfected with pRK5 was used as a positive control.