Evidence for a role of the N-terminal domain in subcellular localization of the neuronal connexin36 (Cx36)

G. Zoidl, C. Meier, E. Petrasch-Parwez, C. Zoidl, H. W. Habbes, M. Kremer, M. Srinivas, D. C. Spray, R. Dermietzel

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


The expression and functional properties of connexin36 (Cx36) have been investigated in two neuroblastoma cell lines (Neuro2A, RT4-AC) and primary hippocampal neurons transfected with a Cx36-enhanced green fluorescent protein (EGFP) expression vector. Transfected cells express Cx36-EGFP mRNA, and Cx36-EGFP protein is localized in the perinuclear area and cell membrane. Upon differentiation of cell lines, Cx36-EGFP protein was detectable in processes with both axonal and dendritic characteristics. Small gap junction plaques were found between adjacent cells, and electrophysiological recordings demonstrated that the electrical properties of these gap junctions were virtually indistinguishable from those reported for native Cx36. Mutagenesis of Cx36 led to the identification of a structural element that interferes with normal protein localization. In contrast, site directed mutagenesis of putative protein phosphorylation motifs did not alter subcellular localization. This excludes phosphorylation/dephosphorylation as a major regulatory step in Cx36 protein transport.

Original languageEnglish (US)
Pages (from-to)448-465
Number of pages18
JournalJournal of Neuroscience Research
Issue number4
StatePublished - Aug 15 2002


  • Coupling
  • Electrical synapse
  • Gap junction
  • Intercellular communication
  • Site directed mutagenesis
  • Trafficking

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience


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