Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases.

Hossain, KR; Clayton, D; Goodchild, SC; Rodger, A; Payne, RJ; Cornelius, F; Clarke, RJ

Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases.

Hossain, KR Clayton, D Goodchild, SC Rodger, A Payne, RJ Cornelius, F Clarke, RJ

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Publisher:: Royal Society of Chemistry
Publication Type:: Journal Article
Citation:: Faraday Discussions, 2021, 232, (0), pp. 172-187
Issue Date:: 2021-12-24

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Field	Value	Language
dc.contributor.author	Hossain, KR
dc.contributor.author	Clayton, D
dc.contributor.author	Goodchild, SC
dc.contributor.author	Rodger, A
dc.contributor.author	Payne, RJ
dc.contributor.author	Cornelius, F
dc.contributor.author	Clarke, RJ
dc.date.accessioned	2022-02-07T02:33:49Z
dc.date.available	2022-02-07T02:33:49Z
dc.date.issued	2021-12-24
dc.identifier.citation	Faraday Discussions, 2021, 232, (0), pp. 172-187
dc.identifier.issn	1359-6640
dc.identifier.issn	1364-5498
dc.identifier.uri	http://hdl.handle.net/10453/154240
dc.description.abstract	Membrane protein structure and function are modulated via interactions with their lipid environment. This is particularly true for integral membrane pumps, the P-type ATPases. These ATPases play vital roles in cell physiology, where they are associated with the transport of cations and lipids, thereby generating and maintaining crucial (electro-)chemical potential gradients across the membrane. Several pumps (Na+, K+-ATPase, H+, K+-ATPase and the plasma membrane Ca2+-ATPase) which are located in the asymmetric animal plasma membrane have been found to possess polybasic (lysine-rich) domains on their cytoplasmic surfaces, which are thought to act as phosphatidylserine (PS) binding domains. In contrast, the sarcoplasmic reticulum Ca2+-ATPase, located within an intracellular organelle membrane, does not possess such a domain. Here we focus on the lysine-rich N-termini of the plasma-membrane-bound Na+, K+- and H+, K+-ATPases. Synthetic peptides corresponding to the N-termini of these proteins were found, via quartz crystal microbalance and circular dichroism measurements, to interact via an electrostatic interaction with PS-containing membranes, thereby undergoing an increase in helical or other secondary structure content. As well as influencing ion pumping activity, it is proposed that this interaction could provide a mechanism for sensing the lipid asymmetry of the plasma membrane, which changes drastically when a cell undergoes apoptosis, i.e. programmed cell death. Thus, polybasic regions of plasma membrane-bound ion pumps could potentially perform the function of a "death sensor", signalling to a cell to reduce pumping activity and save energy.
dc.format	Electronic
dc.language	eng
dc.publisher	Royal Society of Chemistry
dc.relation.ispartof	Faraday Discussions
dc.relation.isbasedon	10.1039/d0fd00040j
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	03 Chemical Sciences
dc.subject.classification	Chemical Physics
dc.title	Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases.
dc.type	Journal Article
utslib.citation.volume	232
utslib.location.activity	England
utslib.for	03 Chemical Sciences
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	closed_access	*
pubs.consider-herdc	false
dc.date.updated	2022-02-07T02:33:47Z
pubs.issue	0
pubs.publication-status	Published
pubs.volume	232
utslib.citation.issue	0

Abstract:

Membrane protein structure and function are modulated via interactions with their lipid environment. This is particularly true for integral membrane pumps, the P-type ATPases. These ATPases play vital roles in cell physiology, where they are associated with the transport of cations and lipids, thereby generating and maintaining crucial (electro-)chemical potential gradients across the membrane. Several pumps (Na+, K+-ATPase, H+, K+-ATPase and the plasma membrane Ca2+-ATPase) which are located in the asymmetric animal plasma membrane have been found to possess polybasic (lysine-rich) domains on their cytoplasmic surfaces, which are thought to act as phosphatidylserine (PS) binding domains. In contrast, the sarcoplasmic reticulum Ca2+-ATPase, located within an intracellular organelle membrane, does not possess such a domain. Here we focus on the lysine-rich N-termini of the plasma-membrane-bound Na+, K+- and H+, K+-ATPases. Synthetic peptides corresponding to the N-termini of these proteins were found, via quartz crystal microbalance and circular dichroism measurements, to interact via an electrostatic interaction with PS-containing membranes, thereby undergoing an increase in helical or other secondary structure content. As well as influencing ion pumping activity, it is proposed that this interaction could provide a mechanism for sensing the lipid asymmetry of the plasma membrane, which changes drastically when a cell undergoes apoptosis, i.e. programmed cell death. Thus, polybasic regions of plasma membrane-bound ion pumps could potentially perform the function of a "death sensor", signalling to a cell to reduce pumping activity and save energy.

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http://hdl.handle.net/10453/154240