| First Author | Boczonadi V | Year | 2012 |
| Journal | FEBS Lett | Volume | 586 |
| Issue | 19 | Pages | 3090-6 |
| PubMed ID | 22841549 | Mgi Jnum | J:188710 |
| Mgi Id | MGI:5441650 | Doi | 10.1016/j.febslet.2012.07.057 |
| Citation | Boczonadi V, et al. (2012) Annexin A9 is a periplakin interacting partner in membrane-targeted cytoskeletal linker protein complexes. FEBS Lett 586(19):3090-6 |
| abstractText | Periplakin regulates keratin organisation and participates in the assembly of epidermal cornified envelopes. A proteomic approach identified annexin A9 as a novel interacting partner for periplakin N-terminus. The presence of annexin A9 in complexes with periplakin was confirmed by immunoblotting of proteins immunoprecipitated by anti-HA or anti-annexin A9 antibodies. Both endogenous and GFP-tagged annexin A9 co-localise with endogenous periplakin and transfected periplakin N-terminus at MCF-7 cell borders and aggregate after Okadaic acid treatment. Annexin A9 and periplakin co-localise in the epidermis and annexin A9 is up-regulated in differentiating keratinocytes, but the epidermal annexin A9 expression does not require periplakin. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: Annexin-9physically interacts with Periplakin by anti bait co-immunoprecipitation (View interaction) Periplakinphysically interacts with Annexin-9 by anti tag co-immunoprecipitation (View Interaction: 1, 2) Periplakin and Annexin-9colocalize by fluorescence microscopy (View Interaction: 1, 2, 3) Keratin-8 and Periplakincolocalize by fluorescence microscopy (View interaction). |
