Proteomics

Dataset Information

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CDK9 interacts with a RanGTP-NEMP1-Importin-β complex to regulate erythroid enucleation


ABSTRACT: Erythroid enucleation is the final stage of erythroid terminal differentiation and involves the separation of an orthochromatic erythroblast into two daughter cells; a pyrenocyte containing the extruded nucleus, and a reticulocyte that will become a red blood cell. Our previous work identified CDK9 as a regulator of erythroid enucleation that appears to act independently of its known role in regulating RNA polymerase II transcription, suggesting the potential for a new CDK9 role. Using a co-immunoprecipitation and mass spectrometry approach, we identified the interactome of CDK9 in differentiating erythroblasts. We show that CDK9 interacts with a RanGTP-NEMP1-Importin-β complex during erythroid terminal differentiation, and inhibition of importin-β in erythroblasts blocks erythroid enucleation. Using imaging analysis and functional assays of enucleating erythroblasts, we show that CDK9 and importin-β co-locate at a critical site of activity opposite to the nucleus before nuclear extrusion and we describe a novel finding that physically links CDK9 and importin-β activity prior to CaM/Ca2+ signalling and subsequent F-actin activity to achieve enucleation.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Erythrocyte, Cell Culture

DISEASE(S): Disease Free

SUBMITTER: Rohan Lowe  

LAB HEAD: Patrick O. Humbert

PROVIDER: PXD072077 | Pride | 2026-04-01

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
H2_D168N_CDK9_1_20230330215000.raw Raw
H2_D168N_CDK9_2_20230331073825.raw Raw
H2_D168N_CDK9_3.raw Raw
H2_D168N_IgG1.raw Raw
H2_D168N_IgG2_20230331024415.raw Raw
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