Acidic leucine-rich nuclear phosphoprotein 32 family member B

Definition:

Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription. Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis. Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes. Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1. Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity).; (Microbial infection) Plays an essential role in influenza A and B viral genome replication. Also plays a role in foamy virus mRNA export from the nucleus to the cytoplasm.

References:

[1]. Jochen Bodem, et al. Foamy virus nuclear RNA export is distinct from that of other retroviruses. J Virol. 2011 Mar;85(5):2333-41. [Content Brief]

[2]. Ecco Staller, et al. ANP32 Proteins Are Essential for Influenza Virus Replication in Human Cells. J Virol. 2019 Aug 13;93(17):e00217-19. [Content Brief]

[3]. Barbara Fries, et al. Analysis of nucleocytoplasmic trafficking of the HuR ligand APRIL and its influence on CD83 expression. J Biol Chem. 2007 Feb 16;282(7):4504-4515. [Content Brief]

[4]. Zhenyu Zhang, et al. Selective usage of ANP32 proteins by influenza B virus polymerase: Implications in determination of host range. PLoS Pathog. 2020 Oct 12;16(10):e1008989. [Content Brief]

[5]. Yoshiko Munemasa, et al. Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5. Mol Cell Biol. 2008 Feb;28(3):1171-81. [Content Brief]

[6]. Naoya Tochio, et al. Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain. J Mol Biol. 2010 Aug 6;401(1):97-114. [Content Brief]

[7]. Shao-Ming Shen, et al. Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells. Carcinogenesis. 2010 Mar;31(3):419-26. [Content Brief]

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