On the structure and mechanism of two‐pore channels
Abstract
In eukaryotes, two‐pore channels ( TPC 1–3) comprise a family of ion channels that regulate the conductance of Na + and Ca 2+ ions across cellular membranes. TPC 1–3 form endolysosomal channels, but TPC 3 can also function in the plasma membrane. TPC 1/3 are voltage‐gated channels, but TPC 2 opens in response to binding endolysosome‐specific lipid phosphatidylinositol‐3,5‐diphosphate ( PI (3,5)P 2 ). Filoviruses, such as Ebola, exploit TPC ‐mediated ion release as a means of escape from the endolysosome during infection. Antagonists that block TPC 1/2 channel conductance abrogate filoviral infections. TPC 1/2 form complexes with the mechanistic target of rapamycin complex 1 ( mTORC 1) at the endolysosomal surface that couple cellular metabolic state and cytosolic nutrient concentrations to the control of membrane potential and pH . We determined the X‐ray structure of TPC 1 from Arabidopsis thaliana (At TPC 1) to 2.87Å resolution—one of the two first reports of a TPC channel structure. Here, we summarize these findings and the implications that the structure may have for understanding endolysosomal control mechanisms and their role in human health.
- Authors:
-
[1];
- Department of Biochemistry and Biophysics University of California San Francisco CA USA
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1401326
- Resource Type:
- Publisher's Accepted Manuscript
- Journal Name:
- Federation of European Biochemical Societies (FEBS) Journal
- Additional Journal Information:
- Journal Name: Federation of European Biochemical Societies (FEBS) Journal Journal Volume: 285 Journal Issue: 2; Journal ID: ISSN 1742-464X
- Publisher:
- Wiley-Blackwell
- Country of Publication:
- United Kingdom
- Language:
- English
Citation Formats
Kintzer, Alexander F., and Stroud, Robert M. On the structure and mechanism of two‐pore channels. United Kingdom: N. p., 2017.
Web. doi:10.1111/febs.14154.
Kintzer, Alexander F., & Stroud, Robert M. On the structure and mechanism of two‐pore channels. United Kingdom. https://doi.org/10.1111/febs.14154
Kintzer, Alexander F., and Stroud, Robert M. Tue .
"On the structure and mechanism of two‐pore channels". United Kingdom. https://doi.org/10.1111/febs.14154.
@article{osti_1401326,
title = {On the structure and mechanism of two‐pore channels},
author = {Kintzer, Alexander F. and Stroud, Robert M.},
abstractNote = {In eukaryotes, two‐pore channels ( TPC 1–3) comprise a family of ion channels that regulate the conductance of Na + and Ca 2+ ions across cellular membranes. TPC 1–3 form endolysosomal channels, but TPC 3 can also function in the plasma membrane. TPC 1/3 are voltage‐gated channels, but TPC 2 opens in response to binding endolysosome‐specific lipid phosphatidylinositol‐3,5‐diphosphate ( PI (3,5)P 2 ). Filoviruses, such as Ebola, exploit TPC ‐mediated ion release as a means of escape from the endolysosome during infection. Antagonists that block TPC 1/2 channel conductance abrogate filoviral infections. TPC 1/2 form complexes with the mechanistic target of rapamycin complex 1 ( mTORC 1) at the endolysosomal surface that couple cellular metabolic state and cytosolic nutrient concentrations to the control of membrane potential and pH . We determined the X‐ray structure of TPC 1 from Arabidopsis thaliana (At TPC 1) to 2.87Å resolution—one of the two first reports of a TPC channel structure. Here, we summarize these findings and the implications that the structure may have for understanding endolysosomal control mechanisms and their role in human health.},
doi = {10.1111/febs.14154},
journal = {Federation of European Biochemical Societies (FEBS) Journal},
number = 2,
volume = 285,
place = {United Kingdom},
year = {Tue Jul 25 00:00:00 EDT 2017},
month = {Tue Jul 25 00:00:00 EDT 2017}
}
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