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PRISMA screen on pathogenic mutations that destroy phosphorylation sites within intrinsically disordered regions

ABSTRACT: Many of the disease-causing point mutations occur within structure-lacking intrinsically disordered regions (IDRs) of proteins. IDRs often contain short linear motifs (SLiMs) that are crucial for protein-protein interactions (PPIs) and are often subject to phosphorylation. Our approach involved immobilizing synthetic peptides representing mutated phosphorylation sites within the IDR regions onto cellulose membranes to capture interacting proteins from cellular extracts. This enabled simultaneous comparison of interaction partners between wild-type, phosphorylated, and mutated peptide forms, allowing functional assessment of individual mutations. We screened 36 disease-causing phosphorylation site mutations within IDRs, sourced from PTMVar database. The results revealed substantial differences between phosphorylated and mutated peptide interactomes, often due to disrupted phosphorylated SLiMs

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Trendelina Rrustemi

LAB HEAD: Matthias Selbach

PROVIDER: PXD043787 | Pride | 2024-02-15

REPOSITORIES: Pride

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			Action	DRS
	180710_KM_PepArray_001_180730204854.raw	Raw
	180710_KM_PepArray_002_180730232514.raw	Raw
	180710_KM_PepArray_003_180731015931.raw	Raw
	180710_KM_PepArray_004_180731043354.raw	Raw
	180710_KM_PepArray_005_180731070811.raw	Raw

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