Multiple pathways in the trafficking and assembly of connexin 26, 32 and 43 into gap junction intercellular communication channels

• DOI: 10.1242/jcs.114.21.3845
• Publication Date: 2021-04-26T00:27:41Z
• Authors: Patricia E. M. Ma...; Geraldine Blundell; Shoeb Ahmad; Rachel J. Errington; W. Howard Evans
• Keywords: Brefeldin A; Nocodazole

The assembly of gap junctions was investigated in mammalian cells expressing connexin (Cx) 26, 32 and 43 fused to green, yellow or cyan fluorescent proteins (GFP, YFP, CFP). Targeting Cx32-CFP 43-GFP junctional communication inhibited treated with Brefeldin A, a drug that disassembles the Golgi. However constructed Cx26-GFP were only minimally affected by A. Nocodazole, microtubule disruptor, had little effect on Cx43-GFP junctions, but perturbed junctions. Co-expression Cx26-YFP A resulted Cx26-YFP. Two amino acids distinguish Cx26 from Cx32 transmembrane domains mutated investigate underlying mechanisms determining trafficking routes One mutation, Cx32I28L, conferred it partial Cx26-like properties as well post-translational membrane insertion characteristics Cx26, suggesting key determinant regulating present first domain. results provide protein basis for specifying composition thus selectivity intercellular signaling, through secretory pathway also following an alternative pathway.