PXD059651

PXD059651 is an original dataset announced via ProteomeXchange.

Title	Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.
Description	In plant cells, the ALMTs are key plasma and vacuolar membranes anion channels regulating plant responses to the environment. Vacuolar ALMTs control stomata aperture and anion accumulation in guard cells. The activation of vacuolar ALMTs is voltage and malate dependent, but the underlying mechanisms remain elusive. Here we report the cryo-EM structure of ALMT9 from Arabidopsis thaliana (AtALMT9), a malate-activated vacuolar anion channel in various lipid-bound states. In all the states, lipids interact with the ion conduction pore of AtALMT9. We found lipid-bound states in plugged and unplugged conformations. Two unplugged states represent with distinct pore width profiles. Structural and functional analysis identified conserved residues involved in ion conduction and pore lipid plugging. Molecular dynamic simulations revealed a peculiar anion conduction mechanism in AtALMT9. We propose a voltage dependent activation mechanism based on the competition between pore-lipids and malate at the cytosolic entrance of the channel
HostingRepository	PRIDE
AnnounceDate	2025-03-04
AnnouncementXML	Submission_2025-03-04_07:05:05.232.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Seoyoung Jang
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	No PTMs are included in the dataset
Instrument	timsTOF Pro 2

Revision	Datetime	Status	ChangeLog Entry
0	2025-01-10 12:31:44	ID requested
⏵ 1	2025-03-04 07:05:06	announced

10.1038/s41467-025-56940-5;

Lee Y, Demes-Causse E, Yoo J, Jang SY, Jung S, Ja, ś, lan J, Hwang GS, Yoo J, De Angeli A, Lee S, Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9. Nat Commun, 16(1):1817(2025) [pubmed]

submitter keyword: ALMT9, lipid, LC-MS/MS

Geum-Sook Hwang
contact affiliation	Integrated Metabolomics Research Group, Metropolitan Seoul Center, Korea Basic Science Institute, Republic of Korea
contact email	gshwang@kbsi.re.kr
lab head
Seoyoung Jang
contact affiliation	Korea Basic Science Institute
contact email	jm0326@kbsi.re.kr
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/03/PXD059651

PRIDE project URI

• PRIDE
  1. PXD059651
     1. Label: PRIDE project
     2. Name: Structural basis for malate-driven, pore lipid-regulated activation of the Arabidopsis vacuolar anion channel ALMT9.