scispace - formally typeset
N

Nouf N. Laqtom

Researcher at King Abdulaziz University

Publications -  16
Citations -  1347

Nouf N. Laqtom is an academic researcher from King Abdulaziz University. The author has contributed to research in topics: Lysosome & Medicine. The author has an hindex of 7, co-authored 10 publications receiving 883 citations. Previous affiliations of Nouf N. Laqtom include University of Edinburgh & Massachusetts Institute of Technology.

Papers
More filters
Journal ArticleDOI

Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes

TL;DR: In this article, a method for the rapid isolation of mammalian lysosomes and use it to quantitatively profile lyssomal metabolites under various cell states was described. And the results reveal the dynamic nature of LSA metabolites and that V-ATPase-and mTOR-dependent mechanisms exist for controlling LSA amino acid efflux.

Lysosomal metabolomics reveals V-ATPase- and mTOR-dependent regulation of amino acid efflux from lysosomes

TL;DR: Analysis of the contents of cultured human cells showed that efflux from the lysosome of most essential amino acids (but not that of most other amino acids) is a regulated process, and that V-ATPase- and mTOR-dependent mechanisms exist for controlling lysOSomal amino acid efflux.
Journal ArticleDOI

NUFIP1 is a ribosome receptor for starvation-induced ribophagy

TL;DR: It is proposed that NUFIP1 is a receptor for the selective autophagy of ribosomes, and nutrient levels and mTOR dynamically modulate the lysosomal proteome.
Journal ArticleDOI

Induction of IL-4Rα-dependent microRNAs identifies PI3K/Akt signaling as essential for IL-4-driven murine macrophage proliferation in vivo

TL;DR: Identification of miR-378-3p as an IL-4Rα-induced microRNA led to the discovery that Akt regulates the newly discovered mechanism ofIL-4-driven macrophage proliferation, suggesting that negative regulation of Akt signaling via microRNAs might play a central role in limiting MΦ expansion and alternative activation during type 2 inflammatory settings.
Journal ArticleDOI

Structural basis for the docking of mTORC1 on the lysosomal surface

TL;DR: The structure shows why Raptor binds only to a specific nucleotide conformation of the Rag heterodimer and suggests a model for how mTORC1 would dock onto the lysosomal surface, which is a key step in its activation.