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Fig. 11 | BMC Cell Biology

Fig. 11

From: Molecular mechanisms regulating formation, trafficking and processing of annular gap junctions

Fig. 11

Scheme depicting how access of clathrin to Cx43 might be regulated. a Interestingly, all proposed Cx43 modifications relevant to Cx43 gap junction internalization cluster into two domains, ‘early’ occurring on residues located juxtaposed to the C-terminal ZO-1 binding site (shaded green), and ‘late’ occurring on residues located juxtaposed to the S2, S3 AP-2 (Eps 15)/clathrin binding sites (shaded red). The lowest energy 3D solution NMR structure of the Cx43-CT revealing the location of critical residues solved by Sorgen and colleagues [117] is shown. b We propose that a conformational change of the Cx43-C-terminal domain (CT) triggered by serine 365 de-phosphorylation [116] opens up the Cx43-CT allowing MAPK to access and phosphorylate S279/282 (and eventually also S262 and S255); and E3-ubiquitin ligases to bind to and ubiquitinate Cx43 (presumably on lysine 303) to promote AP-2 (and/or Eps15) to access the YXXΦ -binding motifs (S2, 265YAYF268; S3, 286YKLV289), recruit clathrin and internalize gap junctions/central gap junction plaque portions

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