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Ubiquitin remnant analysis in melanoma post inhibition of Usp9x

ABSTRACT: Assay the ubiquitinated protein remmants post depletion or inhibition of the deubiquitinase Usp9x in melanoma cells.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Melanoma

SUBMITTER: Luke Peterson

LAB HEAD: Luke Peterson

PROVIDER: PXD005417 | Pride | 2017-02-20

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	092514_22696_Control_1_MS_v.RAW	Raw
	092514_22696_Control_1_MS_v.mzXML	Mzxml
	092514_22697_Control_2_MS_v.RAW	Raw
	092514_22697_Control_2_MS_v.mzXML	Mzxml
	092514_22698_Usp9x_KD1_MS_v.RAW	Raw

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1 - 5 of 19

Publications

Usp9x regulates Ets-1 ubiquitination and stability to control NRAS expression and tumorigenicity in melanoma.

Potu Harish H Peterson Luke F LF Kandarpa Malathi M Pal Anupama A Sun Hanshi H Durham Alison A Harms Paul W PW Hollenhorst Peter C PC Eskiocak Ugur U Talpaz Moshe M Donato Nicholas J NJ

Nature communications 20170215

ETS transcription factors are commonly deregulated in cancer by chromosomal translocation, overexpression or post-translational modification to induce gene expression programs essential in tumorigenicity. Targeted destruction of these proteins may have therapeutic impact. Here we report that Ets-1 destruction is regulated by the deubiquitinating enzyme, Usp9x, and has major impact on the tumorigenic program of metastatic melanoma. Ets-1 deubiquitination blocks its proteasomal destruction and enh ...[more]

PMID: 28198367

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