Proteomics

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BioID proximity biotinylation-MS analysis of human main RAS GTPases in K-562 CML cells


ABSTRACT: The human main RAS GTPases (KRAS4A, KRAS4B, NRAS and HRAS) represent major hubs of cellular signal transduction and are highly mutated in various different cancer entities. RAS GTPases are tightly controlled via different molecular mechanisms in order to coordinate their cellular signaling activity integrating extracellular and intracellular signals. In order to identify novel regulators of RAS signaling activity we have devised a BioID (BirA*-based proximity biotinylation)-Mass spectrometry-based approach in the human K-562 CML cell line. The deposited data set contains the acquired MS data after inducible expression, biotinylation, purification and proteomic analysis of KRAS4A, KRAS4B, NRAS and HRAS proteins. Further detailed information can be found in the appended sample data sheet and in the material and methods section of the manuscript Bigenzahn et al..

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Cell, Cell Culture

DISEASE(S): Chronic Myeloid Leukemia

SUBMITTER: Johannes Bigenzahn  

LAB HEAD: Giulio Superti-Furga

PROVIDER: PXD011280 | Pride | 2018-12-03

REPOSITORIES: Pride

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Publications


In genetic screens aimed at understanding drug resistance mechanisms in chronic myeloid leukemia cells, inactivation of the cullin 3 adapter protein-encoding leucine zipper-like transcription regulator 1 (<i>LZTR1</i>) gene led to enhanced mitogen-activated protein kinase (MAPK) pathway activity and reduced sensitivity to tyrosine kinase inhibitors. Knockdown of the <i>Drosophila LZTR1</i> ortholog <i>CG3711</i> resulted in a Ras-dependent gain-of-function phenotype. Endogenous human LZTR1 assoc  ...[more]

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