Proteomics

Dataset Information

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Analysis of mng-SHIP1-dCT with pY Peptide by HDX-MS

ABSTRACT: Hydrogen deuterium exchange mass spectrometry (HDX-MS) was used to analyze how the mng-SHIP1-dCT construct interacts receptor-derived phosphotryrosine peptides (pY) to probe how these peptides regulate SHIP1 autoinhibition. This HDX-MS helped to identify intramolecular contacts involved in the regulation of SHIP1 autoinibition. Results from this HDX analyzing the dimeric mng-SHIP1 construct are used in tandem with previous results analyzing the monomeric mini-SHIP construct to confirm the same mechanism of autoinhibtion exists. These results help confirm autoinhibition of monomeric SHIP1 is indeed likely regulated by the same mechanism to that of dimeric SHIP1.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD058704 | Pride | 2025-10-15

REPOSITORIES: Pride

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Dataset's files

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Action DRS
10_24_24_HN21_P_3s-1.d.rar Other
10_24_24_HN21_S-MSMS.d.rar Other
10_24_24_HN21_S-ND.d.rar Other
10_24_24_HN21_S_3s-1.d.rar Other
10_25_24_HN21_P_3000s-1.d.rar Other
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Publications

SH2-mediated steric occlusion of the C2 domain regulates autoinhibition of SHIP1 inositol 5-phosphatase.

Drew Emma E EE   Nyvall Hunter G HG   Parson Matthew A H MAH   Talus Reed K RK   Burke John E JE   Hansen Scott D SD  

The Journal of biological chemistry 20251006

The Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1 (SHIP1) is an immune cell specific enzyme that regulates phosphatidylinositol-(3,4,5)-trisphosphate signaling at the plasma membrane following receptor activation. SHIP1 plays an important role in processes such as directed cell migration, endocytosis, and cortical membrane oscillations. Alterations in SHIP1 expression have been shown to perturb myeloid cell chemotaxis and differentiation. In the brain, SHIP1 regul  ...[more]

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