PMID- 17972320
OWN - NLM
STAT- MEDLINE
DCOM- 20080423
LR  - 20231213
IS  - 1097-4547 (Electronic)
IS  - 0360-4012 (Print)
IS  - 0360-4012 (Linking)
VI  - 86
IP  - 5
DP  - 2008 Apr
TI  - Cx29 and Cx32, two connexins expressed by myelinating glia, do not interact and 
      are functionally distinct.
PG  - 992-1006
AB  - In rodents, oligodendrocytes and myelinating Schwann cells express connexin32 
      (Cx32) and Cx29, which have different localizations in the two cell types. We 
      show here that, in contrast to Cx32, Cx29 does not form gap junction plaques or 
      functional gap junctions in transfected cells. Furthermore, when expressed 
      together, Cx29 and Cx32 are not colocalized and do not coimmunoprecipitate. To 
      determine the structural basis of their divergent behavior, we generated a series 
      of chimeric Cx32-Cx29 proteins by exchanging their intracellular loops and/or 
      their C-terminal cytoplasmic tails. Although some chimerae reach the cell 
      membrane, others appear to be largely localized intracellularly; none form gap 
      junction plaques or functional gap junctions. Substituting the C-terminus or the 
      intracellular loop and the C-terminus of Cx32 with those of Cx29 does not disrupt 
      their colocalization or coimmunoprecipitation with Cx32. Substituting the 
      C-terminus of Cx29 with that of Cx32 does not disrupt the coimmunoprecipitation 
      or the colocalization with Cx29, whereas substituting both the intracellular loop 
      and the C-terminus of Cx32 with those of Cx29 diminishes the 
      coimmunoprecipitation with Cx29. Conversely, the Cx32 chimera that contains the 
      intracellular loop of Cx29 coimmunoprecipitates with Cx29, indicating that the 
      intracellular loop participates in Cx29-Cx29 interactions. These data indicate 
      that homomeric interactions of Cx29 and especially Cx32 largely require other 
      domains: the N-terminus, transmembrane domains, and extracellular loops. 
      Substituting the intracellular loop and/or tail of Cx32 with those of Cx29 
      appears to prevent Cx32 from forming functional gap junctions.
FAU - Ahn, Meejin
AU  - Ahn M
AD  - Department of Neurology, University of Pennsylvania School of Medicine, 
      Philadelphia, Pennsylvania 19104-6077, USA.
FAU - Lee, Jonathan
AU  - Lee J
FAU - Gustafsson, Andreas
AU  - Gustafsson A
FAU - Enriquez, Alan
AU  - Enriquez A
FAU - Lancaster, Eric
AU  - Lancaster E
FAU - Sul, Jai-Yoon
AU  - Sul JY
FAU - Haydon, Philip G
AU  - Haydon PG
FAU - Paul, David L
AU  - Paul DL
FAU - Huang, Yan
AU  - Huang Y
FAU - Abrams, Charles K
AU  - Abrams CK
FAU - Scherer, Steven S
AU  - Scherer SS
LA  - eng
GR  - R01 NS055284/NS/NINDS NIH HHS/United States
GR  - K02 NS050345-03/NS/NINDS NIH HHS/United States
GR  - K02 NS050345/NS/NINDS NIH HHS/United States
GR  - R01 NS043560/NS/NINDS NIH HHS/United States
GR  - NS43560/NS/NINDS NIH HHS/United States
GR  - R01 NS042878/NS/NINDS NIH HHS/United States
GR  - NS42878/NS/NINDS NIH HHS/United States
GR  - K02 NS050345-02/NS/NINDS NIH HHS/United States
GR  - P30 NS047321/NS/NINDS NIH HHS/United States
GR  - R01 NS055284-02/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - J Neurosci Res
JT  - Journal of neuroscience research
JID - 7600111
RN  - 0 (Connexins)
RN  - 0 (Gje1 protein, mouse)
RN  - 0 (Mutant Chimeric Proteins)
RN  - 0 (Nerve Tissue Proteins)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cell Differentiation/genetics
MH  - Cell Membrane/metabolism/ultrastructure
MH  - Chlorocebus aethiops
MH  - Connexins/chemistry/genetics/*metabolism
MH  - Gap Junctions/metabolism/ultrastructure
MH  - HeLa Cells
MH  - Humans
MH  - Mice
MH  - Mutant Chimeric Proteins/chemistry/genetics/metabolism
MH  - Myelin Sheath/*metabolism/ultrastructure
MH  - Nerve Tissue Proteins/chemistry/genetics/*metabolism
MH  - Nervous System/*growth & development/*metabolism/ultrastructure
MH  - Neuroglia/*metabolism/ultrastructure
MH  - Protein Structure, Tertiary/physiology
MH  - Gap Junction beta-1 Protein
PMC - PMC2663799
MID - NIHMS96020
EDAT- 2007/11/01 09:00
MHDA- 2008/04/24 09:00
PMCR- 2009/04/01
CRDT- 2007/11/01 09:00
PHST- 2007/11/01 09:00 [pubmed]
PHST- 2008/04/24 09:00 [medline]
PHST- 2007/11/01 09:00 [entrez]
PHST- 2009/04/01 00:00 [pmc-release]
AID - 10.1002/jnr.21561 [doi]
PST - ppublish
SO  - J Neurosci Res. 2008 Apr;86(5):992-1006. doi: 10.1002/jnr.21561.