Irf2bp2a regulates terminal granulopoiesis through proteasomal degradation of Gfi1aa in zebrafish.

Irf2bp2a regulates terminal granulopoiesis through proteasomal degradation of Gfi1aa in zebrafish.

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The ubiquitin-proteasome system plays important roles in various biological processes as it degrades the Bike Parts - Pedals - Parts majority of cellular proteins.Adequate proteasomal degradation of crucial transcription regulators ensures the proper development of neutrophils.The ubiquitin E3 ligase of Growth factor independent 1 (GFI1), a key transcription repressor governing terminal granulopoiesis, remains obscure.

Here we report that the deficiency of the ring finger protein Interferon regulatory factor 2 binding protein 2a (Irf2bp2a) leads to an impairment of neutrophils differentiation in zebrafish.Mechanistically, Irf2bp2a functions as a ubiquitin E3 ligase targeting Gfi1aa for proteasomal degradation.Moreover, irf2bp2a gene is repressed by Flower Girl Dress Gfi1aa, thus forming a negative feedback loop between Irf2bp2a and Gfi1aa during neutrophils maturation.

Different levels of GFI1 may turn it into a tumor suppressor or an oncogene in malignant myelopoiesis.Therefore, discovery of certain drug targets GFI1 for proteasomal degradation by IRF2BP2 might be an effective anti-cancer strategy.