Proteomics

Dataset Information

0

Hydrogen Deuterium Exchange of PI4K(530-560) Peptide with Calcineurin

ABSTRACT: we used HDXMS to study if PI4KA(530-560) is able to bind calcineurin. Here we showed a significant protection in deuterium exchange upon binding calcineurin in the wild type state, indicating these proteins are interacting. Using a mutant that should inhibit the interaction (AKASAA), we showed that this mutant does in fact prevent protection by calcineurin.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD044636 | Pride | 2024-09-03

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
07_14_23_AS_PI4K_Mut_Pept_MSMS_0_01_22598.d.rar Other
07_14_23_AS_PI4K_WT_Pept_MSMS_0_01_22592.d.rar Other
07_18_23_ASHDX5_PM_ND_1_0_01_22609.d.rar Other
07_18_23_ASHDX5_P_ND_1_0_01_22606.d.rar Other
07_24_23_ASHDX5_PC_3s_1_0_01_22617.d.rar Other
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Publications

Structure of calcineurin bound to PI4KA reveals dual interface in both PI4KA and FAM126A.

Shaw Alexandria L AL   Suresh Sushant S   Parson Matthew A H MAH   Harris Noah J NJ   Jenkins Meredith L ML   Yip Calvin K CK   Burke John E JE  

Structure (London, England : 1993) 20240830 11

Phosphatidylinositol 4-kinase alpha (PI4KA) maintains the phosphatidylinositol 4-phosphate (PI4P) and phosphatidylserine pools of the plasma membrane. A key regulator of PI4KA is its association into a complex with TTC7 and FAM126 proteins. This complex can be regulated by the CNAβ1 isoform of the phosphatase calcineurin. We previously identified that CNAβ1 directly binds to FAM126A. Here, we report a cryoelectron microscopic (cryo-EM) structure of a truncated PI4KA complex bound to calcineurin,  ...[more]

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