MassIVE MSV000089341

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Characterization of Affinity Purifications of full length MST2 and exon 7 deleted MST2 by mass spectrometry

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Description

Hippo is a tumor suppressor pathway and is related to the regulation of cell proliferation, apoptosis, organ size and tumorigenesis. In mammals, the Hippo pathway core is composed of 4 serine-threonine kinases: Mammalian Ste-20-like Kinase 1 and 2 (MST1 and MST2) and large suppressive tumor 1 and 2 (LATS1 and LATS2). When Hippo is active, the transcription co-activators YAP and TAZ are phosphorylated and retained in the cytoplasm. However, when the pathway is inactive, YAP and TAZ are not phosphorylated and enter the cell nucleus, where they activate transcription factors, increasing proliferation and inducing malignant phenotype in epithelial cells. Preliminary results from our laboratory showed that in malignant cells (T4-2), STK3 mRNA (gene encoding MST2) is shorter, a result of an exon skipping splicing that excludes exon 7 from the transcript (STK3delexon7). Analysis of RNAseq data from The Cancer Genome Atlas (TCGA) revealed that the variant STK3delexon7 is also found in samples from patients with breast cancer. We observed that with the exclusion of exon 7 the transcript is translated into a protein that is more susceptible to degradation. Therefore, we wanted to characterize the protein complex of the exon 7 excluded transcript and the full-length protein. To this end, we transfected HEK293-T cells with flag tagged version of full length MST2 and MST2 with the deletion of exon-7. We performed affinity purification of these proteins and characterized their binding partners using mass spectrometry. [doi:10.25345/C50000428] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: affinity purification ; MST2 ; Hippo pathway

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Principal Investigators:
(in alphabetical order) 		Beatrix Ueberheide, NYU Grossman School of Medicine, USA
Submitting User: Trixi
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