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Regulation of Connexin-based channels by fatty acids

dc.contributor.authorPuebla C.
dc.contributor.authorRetamal M.A.
dc.contributor.authorAcuña R.
dc.contributor.authorSáez J.C.
dc.date.accessioned2020-09-02T22:25:58Z
dc.date.available2020-09-02T22:25:58Z
dc.date.issued2017
dc.identifier10.3389/fphys.2017.00011
dc.identifier.citation8, JAN, -
dc.identifier.issn1664042X
dc.identifier.urihttps://hdl.handle.net/20.500.12728/5854
dc.descriptionIn this mini-review, we briefly summarize the current knowledge about the effects of fatty acids (FAs) on connexin-based channels, as well as discuss the limited information about the impact FAs may have on pannexins (Panxs). FAs regulate diverse cellular functions, some of which are explained by changes in the activity of channels constituted by connexins (Cxs) or Panxs, which are known to play critical roles in maintaining the functional integrity of diverse organs and tissues. Cxs are transmembrane proteins that oligomerize into hexamers to form hemichannels (HCs), which in turn can assemble into dodecamers to form gap junction channels (GJCs). While GJCs communicate the cytoplasm of contacting cells, HCs serve as pathways for the exchange of ions and small molecules between the intra and extracellular milieu. Panxs, as well as Cx HCs, form channels at the plasma membrane that enable the interchange of molecules between the intra and extracellular spaces. Both Cx- and Panx-based channels are controlled by several post-translational modifications. However, the mechanism of action of FAs on these channels has not been described in detail. It has been shown however that FAs frequently decrease GJC-mediated cell-cell communication. The opposite effect also has been described for HC or Panx-dependent intercellular communication, where, the acute FA effect can be reversed upon washout. Additionally, changes in GJCs mediated by FAs have been associated with post-translational modifications (e.g., phosphorylation), and seem to be directly related to chemical properties of FAs (e.g., length of carbon chain and/or degree of saturation), but this possible link remains poorly understood. © 2017 Puebla, Retamal, Acuña and Sáez.
dc.language.isoen
dc.publisherFrontiers Research Foundation
dc.subjectConnexon
dc.subjectG-protein coupled receptor
dc.subjectGap junction channel
dc.subjectHemichannel
dc.subjectPannexon
dc.subjectconnexin 43
dc.subjectfatty acid
dc.subjectgap junction protein
dc.subjectmembrane protein
dc.subjectmessenger RNA
dc.subjectpannexin
dc.subjectprotein kinase
dc.subjectunclassified drug
dc.subjectfatty acid analysis
dc.subjecthuman
dc.subjectintracellular signaling
dc.subjectmolecular docking
dc.subjectmolecular stability
dc.subjectnonhuman
dc.subjectprotein domain
dc.subjectprotein expression
dc.subjectprotein function
dc.subjectprotein lipid interaction
dc.subjectprotein localization
dc.subjectprotein modification
dc.subjectprotein synthesis
dc.subjectregulatory mechanism
dc.subjectRNA synthesis
dc.subjectShort Survey
dc.subjecttranscription regulation
dc.titleRegulation of Connexin-based channels by fatty acids
dc.typeShort Survey


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