» Articles » PMID: 25156960

Cracking the ANP32 Whips: Important Functions, Unequal Requirement, and Hints at Disease Implications

Overview
Journal Bioessays
Publisher Wiley
Date 2014 Aug 27
PMID 25156960
Citations 48
Authors
Affiliations
Soon will be listed here.
Abstract

The acidic (leucine-rich) nuclear phosphoprotein 32 kDa (ANP32) family is composed of small, evolutionarily conserved proteins characterized by an N-terminal leucine-rich repeat domain and a C-terminal low-complexity acidic region. The mammalian family members (ANP32A, ANP32B, and ANP32E) are ascribed physiologically diverse functions including chromatin modification and remodelling, apoptotic caspase modulation, protein phosphatase inhibition, as well as regulation of intracellular transport. In addition to reviewing the widespread literature on the topic, we present a concept of the ANP32s as having a whip-like structure. We also present hypotheses that ANP32C and other intronless sequences should not currently be considered bona fide family members, that their disparate necessity in development may be due to compensatory mechanisms, that their contrasting roles in cancer are likely context-dependent, along with an underlying hypothesis that ANP32s represent an important node of physiological regulation by virtue of their diverse biochemical activities.

Citing Articles

ANP32e Binds Histone H2A.Z in a Cell Cycle-Dependent Manner and Regulates Its Protein Stability in the Cytoplasm.

Dijkwel Y, Hart-Smith G, Kurscheid S, Tremethick D Mol Cell Biol. 2024; 44(2):72-85.

PMID: 38482865 PMC: 10950284. DOI: 10.1080/10985549.2024.2319731.


Avian ANP32A incorporated in avian influenza A virions promotes interspecies transmission by priming early viral replication in mammals.

Na L, Sun L, Yu M, Zhang Y, Zhang Y, Zhang Z Sci Adv. 2024; 10(5):eadj4163.

PMID: 38295177 PMC: 10830118. DOI: 10.1126/sciadv.adj4163.


ANP32B promotes colorectal cancer cell progression and reduces cell sensitivity to PRAP1 inhibitor through up-regulating HPF1.

Yang L, Li M, Huang W, Ren P, Yan Q, Hao Y Heliyon. 2024; 10(1):e23829.

PMID: 38192816 PMC: 10772160. DOI: 10.1016/j.heliyon.2023.e23829.


Defining the minimal components of the influenza A virus replication machinery via an in vitro reconstitution system.

Zhu Z, Fan H, Fodor E PLoS Biol. 2023; 21(11):e3002370.

PMID: 37943954 PMC: 10662765. DOI: 10.1371/journal.pbio.3002370.


Existing Evidence for Influenza B Virus Adaptations to Drive Replication in Humans as the Primary Host.

Pekarek M, Weaver E Viruses. 2023; 15(10).

PMID: 37896807 PMC: 10612074. DOI: 10.3390/v15102032.


References
1.
Yan N, Cherepanov P, Daigle J, Engelman A, Lieberman J . The SET complex acts as a barrier to autointegration of HIV-1. PLoS Pathog. 2009; 5(3):e1000327. PMC: 2644782. DOI: 10.1371/journal.ppat.1000327. View

2.
Higashino F, Aoyagi M, Takahashi A, Ishino M, Taoka M, Isobe T . Adenovirus E4orf6 targets pp32/LANP to control the fate of ARE-containing mRNAs by perturbing the CRM1-dependent mechanism. J Cell Biol. 2005; 170(1):15-20. PMC: 2171388. DOI: 10.1083/jcb.200405112. View

3.
Reilly P, Afzal S, Wakeham A, Haight J, You-Ten A, Zaugg K . Generation and characterization of the Anp32e-deficient mouse. PLoS One. 2010; 5(10):e13597. PMC: 2964292. DOI: 10.1371/journal.pone.0013597. View

4.
Schneider R, Bannister A, Weise C, Kouzarides T . Direct binding of INHAT to H3 tails disrupted by modifications. J Biol Chem. 2004; 279(23):23859-62. DOI: 10.1074/jbc.C400151200. View

5.
Schafer Z, Parrish A, Wright K, Margolis S, Marks J, Deshmukh M . Enhanced sensitivity to cytochrome c-induced apoptosis mediated by PHAPI in breast cancer cells. Cancer Res. 2006; 66(4):2210-8. DOI: 10.1158/0008-5472.CAN-05-3923. View