Abstract:
:Connexin 43 (Cx43)-hemichannel activity is controlled by intramolecular interactions between cytoplasmic loop and C-terminal tail. We previously identified the last 10 amino acids of the C-terminal tail of Cx43 as essential for Cx43-hemichannel activity. We developed a cell-permeable peptide covering this sequence (TAT-Cx43CT). In this study, we examined the critical molecular determinants in TAT-Cx43CT to restore Cx43-hemichannel activity. Using amino acid substitutions in TAT-Cx43CT, we identified the two aspartate (Asp378 and Asp379) and two proline (Pro375 and Pro377) residues as critical for TAT-Cx43CT activity, since TAT-Cx43CT(DD/AA) and TAT-Cx43CT(PP/GG) did not overcome the inhibition of Cx43-hemichannel activity induced by thrombin, micromolar cytoplasmic Ca(2+) concentration or truncation of Cx43 at M(239). Consistent with this, we found that biotin-Cx43CT(DD/AA) was much less efficient than biotin-Cx43CT to bind the purified CL domain of Cx43 in surface plasmon resonance experiments. In conclusion, we postulate that Asp378 and Asp379 in the C-terminal part of Cx43 are essential for loop/tail interactions in Cx43 hemichannels, while Pro375 and Pro377 may help to properly coordinate the critical Asp residues.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
D'hondt C,Iyyathurai J,Wang N,Gourdie RG,Himpens B,Leybaert L,Bultynck Gdoi
10.1016/j.bbrc.2013.01.066subject
Has Abstractpub_date
2013-03-22 00:00:00pages
707-12issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(13)00145-9journal_volume
432pub_type
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