Unknown

Dataset Information

0

Questioning the role of selected somatic PIK3C2B mutations in squamous non-small cell lung cancer oncogenesis.


ABSTRACT: PI3K signaling is frequently dysregulated in NSCLC-SQCC. In contrast to well characterized components of the PI3K signaling network contributing to the formation of SQCC, potential oncogenic effects of alterations in PIK3C2B are poorly understood. Here, a large cohort (n = 362) of NSCLC-SQCC was selectively screened for four reported somatic mutations in PIK3C2B via Sanger sequencing. In addition, two mutations leading to an amino acid exchange in the kinase domain (C1181, H1208R) were examined on a functional level. None of the mutations were identified in the cohort while well characterized hotspot PIK3CA mutations were observed at the expected frequency. Ultimately, kinase domain mutations in PI3KC2? were found to have no altering effect on downstream signaling. A set of SQCC tumors sequenced by The Cancer Genome Atlas (TCGA) equally indicates a lack of oncogenic potential of the kinase domain mutations or PIK3C2B in general. Taken together, this study suggests that PIK3C2B might only have a minor role in SQCC oncogenesis.

SUBMITTER: Kind M 

PROVIDER: S-EPMC5663493 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

altmetric image

Publications

Questioning the role of selected somatic PIK3C2B mutations in squamous non-small cell lung cancer oncogenesis.

Kind Marcus M   Klukowska-Rötzler Jolanta J   Berezowska Sabina S   Arcaro Alexandre A   Charles Roch-Philippe RP  

PloS one 20171031 10


PI3K signaling is frequently dysregulated in NSCLC-SQCC. In contrast to well characterized components of the PI3K signaling network contributing to the formation of SQCC, potential oncogenic effects of alterations in PIK3C2B are poorly understood. Here, a large cohort (n = 362) of NSCLC-SQCC was selectively screened for four reported somatic mutations in PIK3C2B via Sanger sequencing. In addition, two mutations leading to an amino acid exchange in the kinase domain (C1181, H1208R) were examined  ...[more]

Similar Datasets

| S-EPMC8643496 | biostudies-literature
| S-EPMC5410347 | biostudies-literature
| S-EPMC2598028 | biostudies-literature
| S-EPMC3499051 | biostudies-literature
| S-EPMC2080626 | biostudies-literature
| S-EPMC5373502 | biostudies-literature
| S-EPMC7377869 | biostudies-literature
| S-EPMC5520508 | biostudies-literature
| S-EPMC7443461 | biostudies-literature
| S-EPMC5308618 | biostudies-literature