Gap junction structures

Makowski, Lee; Caspar, D. L. D.; Phillips, W.C.; Goodenough, D A

doi:10.1016/0022-2836(84)90331-0

Cited by 77 publications

(14 citation statements)

References 37 publications

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“…In a later study, difference maps were generated using 2D crystals of full-length Cx43 GJ channels in an attempt to visualize the intracellular domains (Cheng et al, 2003). The absence of intracellular electron density supported structural disorder in cytoplasmic domains originally suggested by Makowski et al (1984).…”

Section: Gap Junction Structure: High Resolutionsupporting

confidence: 68%

A History of Gap Junction Structure: Hexagonal Arrays to Atomic Resolution

Grosely

Sorgen

2013

Cell Communication & Adhesion

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Gap junctions are specialized membrane structures that provide an intercellular pathway for the propagation and/or amplification of signaling cascades responsible for impulse propagation, cell growth, and development. Prior to the identification of the proteins that comprise gap junctions, elucidation of channel structure began with initial observations of a hexagonal nexus connecting apposed cellular membranes. Concomitant with technological advancements spanning over 50 years, atomic resolution structures are now available detailing channel architecture and the cytoplasmic domains that have helped to define mechanisms governing the regulation of gap junctions. Highlighted in this review are the seminal structural studies that have led to our current understanding of gap junction biology.

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Section: Gap Junction Structure: High Resolutionsupporting

confidence: 68%

A History of Gap Junction Structure: Hexagonal Arrays to Atomic Resolution

Grosely

Sorgen

2013

Cell Communication & Adhesion

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“…It is possible that interhemichannel linkages could form across the intercellular "gap" if the cross-linker could penetrate this intercellular space. The "gap" is known to be penetrated only by heavy metal stains and sucrose, which are smaller than the cross-linkers (5,76). Additionally, due to the relative surface areas available for interaction, under mild cross-linking conditions intrahemichannel linkages would be favored over interhemichannel linkages (77).…”

Section: Co-purification Of Connexin-32 and Connexin-26 -Connexinmentioning

confidence: 99%

Isoform Composition of Connexin Channels Determines Selectivity among Second Messengers and Uncharged Molecules

Bevans¹,

Kordel²,

Rhee³

et al. 1998

Journal of Biological Chemistry

299

255

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Intercellular connexin channels (gap junction channels) have long been thought to mediate molecular signaling between cells, but the nature of the signaling has been unclear. This study shows that connexin channels from native tissue have selective permeabilities, partially based on pore diameter, that discriminate among cytoplasmic second messenger molecules. Permeability was assessed by measurement of selective loss/retention of tracers from liposomes containing reconstituted connexin channels. The tracers employed were tritiated cyclic nucleotides and a series of oligomaltosaccharides derivatized with a small uncharged fluorescent moiety. The data define different size cut-off limits for permeability through homomeric connexin-32 channels and through heteromeric connexin-32/connexin-26 channels. Connexin-26 contributes to a narrowed pore. Both cAMP and cGMP were permeable through the homomeric connexin-32 channels. cAMP was permeable through only a fraction of the heteromeric channels. Surprisingly, cGMP was permeable through a substantially greater fraction of the heteromeric channels than was cAMP. The data suggest that isoform stoichiometry and/or arrangement within a connexin channel determines whether cyclic nucleotides can permeate, and which ones. This is the first evidence for connexin-specific selectivity among biological signaling molecules.

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“…1). The volume of the electron density of a single protein can be used to predict a molecular weight of about 24 kD (Makowski et al, 1984). The discrepancy between this estimate and the values of 27 and 32 kD for the liver gap junction protein gained from protein biochemistry and molecular biology comes from uncertainties in the analysis and proteolysis of the specimens (discussed in Makowski, 1988).…”

Section: Gap Junction Structurementioning

confidence: 99%