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. 2009 Sep 14;18(24):4734–4745. doi: 10.1093/hmg/ddp436

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© The Author 2009. Published by Oxford University Press

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Proteasome markers are upregulated in cells expressing the skin disease mutants and colocalize with the mistrafficked protein. Colocalization studies with the EKV- and neuropathy-associated Cx31 mutants and markers against subcellular compartments known to be involved in connexin assembly and trafficking including the Golgi apparatus (A–D), lysosome (E–H) and the ER (I–L) indicates that the major pool of each of the mistrafficked mutants does not reside in any of these compartments. In contrast, the proteasome marker (Q–T) is upregulated in cells overexpressing the (R42P)Cx31-EGFP (N) and (C86S)Cx31-EGFP (O) mutant, and a degree of colocalization is observed (shown in yellow in V and W). This is not observed in cells overexpressing (WT)Cx31-EGFP (M) or (66delD)Cx31-EGFP (P). EGFP-tagged connexin protein is shown in green. The subcellular marker antibody staining is shown in red. DAPI- stained nuclei are shown in blue.