Proteomics

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Defining the molecular mechanism of PI4KA complex regulation by the phosphatase Calcineurin

ABSTRACT: To examine the interaction between PI4KIIIa and Calcineurin, HDX-MS experiments comparing calcineurin or PI4KA FAM delta C alone to the calcineurin and PI4KA FAM delta C complex were carried out.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E Burke

PROVIDER: PXD043409 | Pride | 2024-09-03

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
03_02_22_SSHDX1_C_3s_1_0_01_18986.d.zip Other
03_02_22_SSHDX1_C_MSMS_0_01_18976.d.mzXML Mzxml
03_02_22_SSHDX1_C_MSMS_0_01_18976.d.zip Other
03_02_22_SSHDX1_C_ND_0_01_18980.d.zip Other
03_02_22_SSHDX1_PC_3s_1_0_01_18984.d.zip 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) 20240822

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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