The kinases c-Src (Giepmans et al. 2001; Sorgen et al. 2004), PKc (Lin et al. 2003) and MAPK (Mograbi et al. 2003) play an essential role in the phosphorylation of Cx which leads to its degradation. c-Src appears to associate with and phosphorylate Cx43 leading to closure of gap junctions. Evidence suggests that v-src may activate MAPK, which in turn phosphorylates Cx43 on serine sites leading to channel gating (Zhou et al. 1999).
|12807735||Aberrant Connexin 43 endocytosis by the carcinogen lindane involves activation of the ERK/mitogen-activated protein kinase pathway||Carcinogenesis||2003|
|10085299||Dissection of the molecular basis of pp60(v-src) induced gating of connexin 43 gap junction channels||J Cell Biol||1999|
|11124251||Interaction of c-Src with gap junction protein connexin-43. Role in the regulation of cell-cell communication.||J Biol Chem||2001|
|14638725||Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts||Invest Ophthalmol Vis Sci||2003|
|15492000||Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1||J Biol Chem||2004|