Proteomics

Dataset Information

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Hydrogen Deuterium Exchange of PIKfyve construct with PI3P vesicles and inhibitors

ABSTRACT: We used HDXMS to study the confomational changes induced in a PIKfyve construct upon binding PI3P membrane and a variety of inhibitors. Here we showed a significant protection in deuterium exchange upon binding all inhibitors, and regions of protection and exposure upon binding PI3P membrane.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD044706 | Pride | 2025-10-15

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
02_09_2023_IBBHDX2_Apo-3000s-1_0_01_21332.d.zip Other
02_09_2023_IBBHDX2_Apo-300s-1_0_01_21328.d.zip Other
02_09_2023_IBBHDX2_Apo-30s-1_0_01_21324.d.zip Other
02_09_2023_IBBHDX2_Apo-3s-1_0_01_21320.d.zip Other
02_09_2023_IBBHDX2_Mem-3000s-1_0_01_21334.d.zip Other
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Publications

An advanced toolset to manipulate and monitor subcellular phosphatidylinositol 3,5-bisphosphate.

Pemberton Joshua G JG   Barlow-Busch Isobel I   Jenkins Meredith L ML   Parson Matthew A H MAH   Sarnyai Farkas F   Bektas Seyma Nur SN   Kim Yeun Ju YJ   Heuser John E JE   Burke John E JE   Balla Tamas T  

The Journal of cell biology 20250326 6

Phosphatidylinositol (PI) 3,5-bisphosphate (PI(3,5)P2) is a minor inositol-containing phospholipid that serves as an important regulator of endolysosomal functions. However, the precise sites of subcellular enrichment and molecular targets of this regulatory lipid are poorly understood. Here, we describe the generation and detailed characterization of a short engineered catalytic fragment of the human PIKfyve enzyme, which potently converts PI 3-phosphate to PI(3,5)P2. This novel tool allowed fo  ...[more]

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