K+ Channel-SEC11 Binding Exchange Regulates SNARE Assembly for Secretory Traffic. Issue 3 (23rd September 2019)
- Record Type:
- Journal Article
- Title:
- K+ Channel-SEC11 Binding Exchange Regulates SNARE Assembly for Secretory Traffic. Issue 3 (23rd September 2019)
- Main Title:
- K+ Channel-SEC11 Binding Exchange Regulates SNARE Assembly for Secretory Traffic
- Authors:
- Waghmare, Sakharam
Lefoulon, Cecile
Zhang, Ben
Liliekyte, Edita
Donald, Naomi
Blatt, Michael R. - Abstract:
- Abstract : K + channels initiate a binding exchange with the SNARE SYP121 to trigger SNARE complex assembly and drive secretory vesicle fusion at the plant plasma membrane. Abstract: Cell expansion requires that ion transport and secretory membrane traffic operate in concert. Evidence from Arabidopsis ( Arabidopsis thaliana ) indicates that such coordination is mediated by physical interactions between subsets of so-called SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which drive the final stages of vesicle fusion, and K + channels, which facilitate uptake of the cation to maintain cell turgor pressure as the cell expands. However, the sequence of SNARE binding with the K + channels and its interweaving within the events of SNARE complex assembly for exocytosis remains unclear. We have combined protein-protein interaction and electrophysiological analyses to resolve the binding interactions of the hetero-oligomeric associations. We find that the RYxxWE motif, located within the voltage sensor of the K + channels, is a nexus for multiple SNARE interactions. Of these, K + channel binding and its displacement of the regulatory protein SEC11 is critical to prime the Qa-SNARE SYP121. Our results indicate a stabilizing role for the Qbc-SNARE SNAP33 in the Qa-SNARE transition to SNARE complex assembly with the R-SNARE VAMP721. They also suggest that, on its own, the R-SNARE enters an anomalous binding mode with the channels, possibly as aAbstract : K + channels initiate a binding exchange with the SNARE SYP121 to trigger SNARE complex assembly and drive secretory vesicle fusion at the plant plasma membrane. Abstract: Cell expansion requires that ion transport and secretory membrane traffic operate in concert. Evidence from Arabidopsis ( Arabidopsis thaliana ) indicates that such coordination is mediated by physical interactions between subsets of so-called SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which drive the final stages of vesicle fusion, and K + channels, which facilitate uptake of the cation to maintain cell turgor pressure as the cell expands. However, the sequence of SNARE binding with the K + channels and its interweaving within the events of SNARE complex assembly for exocytosis remains unclear. We have combined protein-protein interaction and electrophysiological analyses to resolve the binding interactions of the hetero-oligomeric associations. We find that the RYxxWE motif, located within the voltage sensor of the K + channels, is a nexus for multiple SNARE interactions. Of these, K + channel binding and its displacement of the regulatory protein SEC11 is critical to prime the Qa-SNARE SYP121. Our results indicate a stabilizing role for the Qbc-SNARE SNAP33 in the Qa-SNARE transition to SNARE complex assembly with the R-SNARE VAMP721. They also suggest that, on its own, the R-SNARE enters an anomalous binding mode with the channels, possibly as a fail-safe measure to ensure a correct binding sequence. Thus, we suggest that SYP121 binding to the K + channels serves the role of a primary trigger to initiate assembly of the secretory machinery for exocytosis. … (more)
- Is Part Of:
- Plant physiology. Volume 181:Issue 3(2019)
- Journal:
- Plant physiology
- Issue:
- Volume 181:Issue 3(2019)
- Issue Display:
- Volume 181, Issue 3 (2019)
- Year:
- 2019
- Volume:
- 181
- Issue:
- 3
- Issue Sort Value:
- 2019-0181-0003-0000
- Page Start:
- 1096
- Page End:
- 1113
- Publication Date:
- 2019-09-23
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.19.00919 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22688.xml