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. Author manuscript; available in PMC: 2014 Apr 1.
Published in final edited form as: Biosci Rep. 2011 Oct 1;31(5):429–437. doi: 10.1042/BSR20100127

Figure 2. LRRK2 interacts with PTPC members through its ANK-LRR domains.

Figure 2

(A, B) PTPC members interact with the ANK-LRR domains of LRRK2 in vivo. HEK-293 cells were transfected with Flag-LRRK2-M (aa 671–1299) or Flag-LRRK2-C (aa 1212–2527) and various epitope-tagged PTPC members, either alone or in combination as indicated. At 36 h later, cell lysates were immunoprecipitated with an anti-Flag antibody. The immunocomplexes were analysed with an anti-HA antibody. (A) LRRK2 interacts with PTPC members through its ANK-LRR domains. (B) The Roc-COR-kinase-WD40 domains of LRRK2 do not interact with PTPC members. (C) ANK-LRR domains of LRRK2 interact with uMtCK in vitro. GST and GST–uMtCK fusion protein were expressed and purified (lower panel). They were incubated with 35S-labelled Flag-LRRK2-M prepared in an in vitro transcription–translation system for pull-down assays (upper panel). Radioactive proteins that bound to GST–uMtCK were visualized by SDS/PAGE/autoradiography (upper panel).