Proteomics

Dataset Information

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HDX-MS analysis of PI4Ka trimer and FAM126a (415-521) with calcineurin

ABSTRACT: We used HDX-MS to map novel binding sites of calcineurin on PI4KA and FAM126A. Calcineurin binds to PxIxIT and LxVP motifs on PI4KA and FAM126A indicating a novel regulatory mechanism of Pi4KA by calcineurin

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD050633 | Pride | 2024-09-03

REPOSITORIES: Pride

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Dataset's files

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Action DRS
01_26_24_PI4k_CoverageMapping-MSMS.d.rar Other
02_28_24_SS14_P-ND.d.rar Other
02_28_24_SS14_PC_10s-1.d.rar Other
02_28_24_SS14_PC_30s-1.d.rar Other
02_28_24_SS14_PC_3s-1.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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