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Khaoula Belhaj

Researcher at Sainsbury Laboratory

Publications -  6
Citations -  332

Khaoula Belhaj is an academic researcher from Sainsbury Laboratory. The author has contributed to research in topics: Autophagy & Phytophthora infestans. The author has an hindex of 5, co-authored 6 publications receiving 240 citations. Previous affiliations of Khaoula Belhaj include University of East Anglia.

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An effector of the Irish potato famine pathogen antagonizes a host autophagy cargo receptor

TL;DR: It is shown that PexRD54, an effector from the Irish potato famine pathogen Phytophthora infestans, binds host autophagy protein ATG8CL to stimulate autophagosome formation and depletes the autophagic cargo receptor Joka2 out of ATG 8CL complexes and interferes with Joka1's positive effect on pathogen defense.
Journal ArticleDOI

Host autophagy machinery is diverted to the pathogen interface to mediate focal defense responses against the Irish potato famine pathogen.

TL;DR: This work shows that during infection, ATG8CL/Joka2 labelled defense-related autophagosomes are diverted toward the perimicrobial host membrane to restrict pathogen growth, and shows that the host-pathogen interface is a hotspot for autophagy biogenesis.
Journal ArticleDOI

N-terminal β-strand underpins biochemical specialization of an ATG8 isoform.

TL;DR: A comprehensive protein–protein interaction resource is described, obtained using in planta immunoprecipitation followed by mass spectrometry (MS), to define the potato ATG8 interactome, and findings are consistent with the view that ATg8 isoforms comprise a layer of specificity in the regulation of selective autophagy pathways in plants.
Posted ContentDOI

N-terminal β-strand underpins biochemical specialization of an ATG8 isoform

TL;DR: A comprehensive protein-protein interaction resource is described, obtained using in planta immunoprecipitation followed by mass spectrometry, to define the potato ATG8 interactome, and it is found that the N-terminal β-strand—and, in particular, a single amino acid polymorphism—underpins binding specificity to the substrate PexRD54 by shaping the hydrophobic pocket that accommodates this protein’s AtG8 interacting motif.