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Kurlekar, S.

Publications and source records attributed to Kurlekar, S..

3 recordsLinked to original sources

Discrete genetic effects of VHL and PBRM1 inactivation co-operate to disrupt epithelial homeostasis and promote ccRCC

Inactivation of VHL is a truncal alteration in clear cell renal cell carcinoma, but additional events are required for oncogenesis, most commonly PBRM1 inactivation. To better understand this co-operation, we used an oncogenic cell-tagging strategy to analyze the earliest transcriptional and cellular consequences of Vhl and/or Pbrm1 inactivation in the renal tubular epithelium, in vivo, at single-cell resolution. Pbrm1 inactivation did not globally alter HIF-dependent transcription or increase early tubular proliferation induced by Vhl inactivation. Instead, it had independent effects on epithelial organization. Combined genetic and morphological analyses suggested that Pbrm1 inactivation allows cells to sustain Vhl/HIF-dependent proliferation by disrupting tubular architectures that ordinarily restrain this proliferation, resulting in extra-tubular cell accumulation, multilayered epithelia, and tumor formation. Our findings frame a new model for the VHL-PBRM1 interaction that explains loss of epithelial homeostasis through an interaction between discrete effects that drive proliferation and remove structural tissue restraints on that proliferation. Statement of SignificanceVHL and PBRM1 are frequently co-inactivated in ccRCC. Combining transcriptomic and histological analyses of Vhl and/or Pbrm1-inactivated renal cells in vivo, this study highlights independent effects on transcription and epithelial organization that converge to promote sustained proliferation and dysplasia. The work illuminates how tissue homeostasis is disrupted by oncogenic co-operation.

cancer biology↗

HIFalpha isoform specific activities drive cell-type specificity of VHL-associated oncogenesis

Cancers arising from dysregulation of generally operative signaling pathways are often tissue specific, but the mechanisms underlying this paradox are poorly understood. Based on striking cell-type specificity, we postulated that these mechanisms must operate early in cancer development and set out to study them in a model of von Hippel Lindau (VHL) disease. Biallelic mutation of the VHL ubiquitin ligase leads to constitutive activation of hypoxia inducible factors HIF1A and HIF2A and is generally a truncal event in clear cell renal carcinoma. We used an oncogenic tagging strategy in which VHL-mutant cells are marked by tdTomato, enabling their observation, retrieval, and analysis early after VHL-inactivation. Our findings reveal markedly different consequences of HIF1A and HIF2A activation, but that both contribute to renal cell-type specific consequences of VHL-inactivation in the kidney. Early involvement of HIF2A in promoting proliferation within proximal tubular epithelium supports therapeutic targeting of HIF2A early in VHL disease.

cancer biology↗

PP6-regulated Aurora A activity towards NDC80 limits mitotic spindle size to prevent micronucleation

Amplification of the mitotic kinase Aurora A or loss of its regulator protein phosphatase 6 (PP6) have emerged as drivers of genome instability. Cells lacking PPP6C, the catalytic subunit of PP6, have amplified Aurora A activity and as we show here, enlarged mitotic spindles which fail to hold chromosomes tightly together in anaphase, causing defective nuclear structure. Using functional genomics to shed light on the processes underpinning these changes, we discover synthetic lethality between PPP6C and the kinetochore protein NDC80. We find that NDC80 is phosphorylated on multiple N-terminal sites during spindle formation by Aurora A-TPX2, exclusively at checkpoint-silenced, microtubule-attached kinetochores. NDC80 phosphorylation persists until spindle disassembly in telophase, is increased in PPP6C-knockout cells and, and is Aurora B-independent. An Aurora-phosphorylation-deficient NDC80-9A mutant reduces spindle size and suppresses defective nuclear structure in PPP6C-knockout cells. By regulating NDC80 phosphorylation by Aurora A-TPX2, PP6 plays an important role in mitotic spindle formation and size control, and thus the fidelity of cell division.

cell biology↗