PQBP1

Last updated
PQBP1
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PQBP1 , MRX2, MRX55, MRXS3, MRXS8, NPW38, RENS1, SHS, polyglutamine binding protein 1
External IDs OMIM: 300463; MGI: 1859638; HomoloGene: 4172; GeneCards: PQBP1; OMA:PQBP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

10084

54633

Ensembl

ENSG00000102103

ENSMUSG00000031157

UniProt

O60828

Q91VJ5

RefSeq (mRNA)

NM_001252528
NM_001252529
NM_019478

RefSeq (protein)

NP_001239457
NP_001239458
NP_062351

Location (UCSC) Chr X: 48.89 – 48.9 Mb Chr X: 7.76 – 7.77 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Polyglutamine-binding protein 1 (PQBP1) is a protein that in humans is encoded by the PQBP1 gene. [5] [6] [7]

Polyglutamine binding protein-1, which was identified as a binding protein to the polyglutamine tract sequence, [5] [7] is an evolutionally conserved protein [8] expressed in various tissues including developmental [9] and adult brains [7] or mesodermal tissues. [10] In cells, PQBP1 is dominantly located in the nucleus [7] [11] but also in the cytoplasm dependently on the cell type [12] and stress conditions. [13] PQBP1 has recently been found to play a role in the innate immune response of dendritic cells. [14]

It should be of note that PQBP1 has no relationship with QBP1, an artificial synthetic peptide.

Function

PQBP1 is a nuclear polyglutamine-binding protein that contains a WW domain. [7] [15]

The molecular roles of PQBP1 are mainly in mRNA splicing [16] [17] and transcription. [11] [18] PQBP1 interacts with splicing proteins [19] [20] [21] [22] and RNA-binding proteins. [23] [24] PQBP1 deficiency critically affects mRNA splicing of cell cycle and synapse related genes. [16] Recent results indicated implication of PQBP1 in cytoplasmic RNA metabolism [25] and elongation of protein translation from mRNA. [26] Research also seems to suggest that PQBP1 also plays a role in the innate immune system as a necessary adaptor for the cGAS-mediated innate response to lentiviruses such as HIV1. This PQBP-1 dependent response initiates a sensor that detects lentiviral DNA. [27]

Clinical significance

Mutations in the PQBP1 gene, which encodes for this protein, have been known to cause X-linked intellectual disabilities (XLID), commonly referred to as Renpenning's syndrome. [28] Recent studies indicate that PQBP-1 interaction with TXNL4A is missing in patients with frameshift mutations causing Renpenning's syndrome. PQBP-1 seems to facilitate the nuclear import of TXNL4A, however the biological function of that interaction requires further investigation. [29] People who suffer from these disabilities share a common set of symptoms including: microcephaly, shortened stature and impaired intellectual development. [30] There are 11 types of mutations that have been identified, but the most common being frameshift mutations. [28] [31] Other syndromic XLIDs such as Golabi-Ito-Hall syndrome and non-syndromic ID patients were also associated with PQBP1 gene mutations. [32] [33] [34]

Mutant Ataxin-1 and Huntingtin, disease proteins of spinocerebellar ataxia type-1 and Huntington's disease respectively, interact with PQBP1 and disturbed the functions of PQBP1. [11] [35] Moreover, recent investigations revealed pathological roles of PQBP1 in neurons [36] and microglia [12] under neurodegeneration of Alzheimer's disease and tauopathy. SRRM2 phosphorylation detected in neurons at the early stage of Alzheimer's disease pathology [37] leads to reduction of SRRM2, a scaffold protein for RNA metabolism related molecules in the nucleus, which causes reduction of PQBP1 in the nucleus and acquired intellectual disability. [36] PQBP1 was shown as an intracellular receptor for HIV1 in dendritic cells [38] for innate immune system. Recent studies indicate that PQBP1 recognizes intact capsids of HIV-1 particles. It interacts with these capsids through its amino-terminus, and when capsid disassembles it triggers the PQBP-1 dependent recruitment of cGAS. This is crucial to activating the sensor that detects HIV-1 DNA as soon as synthesis is initiated. [27] Similarly, PQBP1 functions as an intracellular receptor for tau proteins and trigger brain inflammation. [12]

Animal models

Mouse models of knockdown and conditional knockout were generated, and they showed cognitive impairment and microcephaly. [39] [16] The KD mice possess a transgene expressing 498 bp double-strand RNA that is endogenously cleaved to siRNA suppressing PQBP1 efficiently, and did not show obvious developmental abnormality. [39] Another knockdown model of the gene in mouse embryo primary neurons revealed a decrease in splicing efficiency and resulted in abnormal gastrulation and neuralation patterning. [10]

Drosophila models of underexpression and overexpression were also generated. [40] [41] The hypomorph Drosophila model revealed molecular function of PQBP1 in learning acquisition mediated by decreased mRNA and protein expressions of NMDA receptor subunit NR1. [40] Research indicates that in order to appropriately function, the protein must be expressed within a critical range. [42] [10]

Related Research Articles

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References

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  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  8. ↑ Okazawa H, Sudol M, Rich T (November 2001). "PQBP-1 (Np/PQ): a polyglutamine tract-binding and nuclear inclusion-forming protein". Brain Research Bulletin. 56 (3–4): 273–280. doi:10.1016/S0361-9230(01)00579-2. PMID   11719261. S2CID   25290878.
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  14. ↑ Yoh SM, Schneider M, Seifried J, Soonthornvacharin S, Akleh RE, Olivieri KC, et al. (June 2015). "PQBP1 Is a Proximal Sensor of the cGAS-Dependent Innate Response to HIV-1". Cell. 161 (6): 1293–1305. doi: 10.1016/j.cell.2015.04.050 . PMC   4503237 . PMID   26046437.
  15. ↑ "OMIM: PQBP1 polyglutamine binding protein 1".
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  17. ↑ Okazawa H (October 2018). "PQBP1, an intrinsically disordered/denatured protein at the crossroad of intellectual disability and neurodegenerative diseases". Neurochemistry International. 119: 17–25. doi: 10.1016/j.neuint.2017.06.005 . PMID   28627366. S2CID   28886506.
  18. ↑ Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H (April 2014). "Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD". Nature Communications. 5: 3822. Bibcode:2014NatCo...5.3822M. doi: 10.1038/ncomms4822 . PMID   24781215.
  19. ↑ Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (October 2000). "Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1". Gene. 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. PMID   11054566.
  20. ↑ Waragai M, Junn E, Kajikawa M, Takeuchi S, Kanazawa I, Shibata M, et al. (July 2000). "PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain". Biochemical and Biophysical Research Communications. 273 (2): 592–595. doi:10.1006/bbrc.2000.2992. PMID   10873650.
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  23. ↑ Komuro A, Saeki M, Kato S (December 1999). "Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine". The Journal of Biological Chemistry. 274 (51): 36513–36519. doi: 10.1074/jbc.274.51.36513 . PMID   10593949.
  24. ↑ Llorian M, Beullens M, Andrés I, Ortiz JM, Bollen M (February 2004). "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1". The Biochemical Journal. 378 (Pt 1): 229–238. doi:10.1042/bj20030950. PMC   1223944 . PMID   14640981.
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  26. ↑ Shen Y, Zhang ZC, Cheng S, Liu A, Zuo J, Xia S, et al. (April 2021). "PQBP1 promotes translational elongation and regulates hippocampal mGluR-LTD by suppressing eEF2 phosphorylation". Molecular Cell. 81 (7): 1425–1438.e10. doi: 10.1016/j.molcel.2021.01.032 . PMID   33662272. S2CID   232122674.
  27. 1 2 Yoh SM, Mamede JI, Lau D, Ahn N, Sánchez-Aparicio MT, Temple J, et al. (August 2022). "Recognition of HIV-1 capsid by PQBP1 licenses an innate immune sensing of nascent HIV-1 DNA". Molecular Cell. 82 (15): 2871–2884.e6. doi:10.1016/j.molcel.2022.06.010. PMC   9552964 . PMID   35809572.
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  29. ↑ Liu X, Dou LX, Han J, Zhang ZC (March 2020). "The Renpenning syndrome-associated protein PQBP1 facilitates the nuclear import of splicing factor TXNL4A through the karyopherin β2 receptor". The Journal of Biological Chemistry. 295 (13): 4093–4100. doi: 10.1074/jbc.RA119.012214 . PMC   7105315 . PMID   32041777.
  30. ↑ Kalscheuer VM, Freude K, Musante L, Jensen LR, Yntema HG, Gécz J, et al. (December 2003). "Mutations in the polyglutamine binding protein 1 gene cause X-linked mental retardation". Nature Genetics. 35 (4): 313–315. doi:10.1038/ng1264. hdl: 11858/00-001M-0000-0010-8953-D . PMID   14634649. S2CID   27007340.
  31. ↑ Germanaud D, Rossi M, Bussy G, Gérard D, Hertz-Pannier L, Blanchet P, et al. (March 2011). "The Renpenning syndrome spectrum: new clinical insights supported by 13 new PQBP1-mutated males". Clinical Genetics. 79 (3): 225–235. doi:10.1111/j.1399-0004.2010.01551.x. PMID   20950397. S2CID   22909872.
  32. ↑ Lubs H, Abidi FE, Echeverri R, Holloway L, Meindl A, Stevenson RE, Schwartz CE (June 2006). "Golabi-Ito-Hall syndrome results from a missense mutation in the WW domain of the PQBP1 gene". Journal of Medical Genetics. 43 (6): e30. doi:10.1136/jmg.2005.037556. PMC   2564547 . PMID   16740914.
  33. ↑ Tapia VE, Nicolaescu E, McDonald CB, Musi V, Oka T, Inayoshi Y, et al. (June 2010). "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing". The Journal of Biological Chemistry. 285 (25): 19391–19401. doi: 10.1074/jbc.M109.084525 . PMC   2885219 . PMID   20410308.
  34. ↑ Sudol M, McDonald CB, Farooq A (August 2012). "Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1". FEBS Letters. 586 (17): 2795–2799. doi:10.1016/j.febslet.2012.03.041. PMC   3413755 . PMID   22710169.
  35. ↑ Busch A, Engemann S, Lurz R, Okazawa H, Lehrach H, Wanker EE (October 2003). "Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: a potential mechanism for loss of huntingtin function in Huntington's disease". The Journal of Biological Chemistry. 278 (42): 41452–41461. doi: 10.1074/jbc.M303354200 . PMID   12888569.
  36. 1 2 Tanaka H, Kondo K, Chen X, Homma H, Tagawa K, Kerever A, et al. (October 2018). "The intellectual disability gene PQBP1 rescues Alzheimer's disease pathology". Molecular Psychiatry. 23 (10): 2090–2110. doi:10.1038/s41380-018-0253-8. PMC   6250680 . PMID   30283027.
  37. ↑ Tagawa K, Homma H, Saito A, Fujita K, Chen X, Imoto S, et al. (January 2015). "Comprehensive phosphoproteome analysis unravels the core signaling network that initiates the earliest synapse pathology in preclinical Alzheimer's disease brain". Human Molecular Genetics. 24 (2): 540–558. doi: 10.1093/hmg/ddu475 . PMID   25231903.
  38. ↑ Yoh SM, Schneider M, Seifried J, Soonthornvacharin S, Akleh RE, Olivieri KC, et al. (June 2015). "PQBP1 Is a Proximal Sensor of the cGAS-Dependent Innate Response to HIV-1". Cell. 161 (6): 1293–1305. doi:10.1016/j.cell.2015.04.050. PMC   4503237 . PMID   26046437.
  39. 1 2 Ito H, Yoshimura N, Kurosawa M, Ishii S, Nukina N, Okazawa H (November 2009). "Knock-down of PQBP1 impairs anxiety-related cognition in mouse". Human Molecular Genetics. 18 (22): 4239–4254. doi: 10.1093/hmg/ddp378 . PMID   19661183.
  40. 1 2 Tamura T, Horiuchi D, Chen YC, Sone M, Miyashita T, Saitoe M, et al. (October 2010). "Drosophila PQBP1 regulates learning acquisition at projection neurons in aversive olfactory conditioning". The Journal of Neuroscience. 30 (42): 14091–14101. doi:10.1523/JNEUROSCI.1319-10.2010. PMC   6634781 . PMID   20962230.
  41. ↑ Yoshimura N, Horiuchi D, Shibata M, Saitoe M, Qi ML, Okazawa H (April 2006). "Expression of human PQBP-1 in Drosophila impairs long-term memory and induces abnormal courtship". FEBS Letters. 580 (9): 2335–2340. doi: 10.1016/j.febslet.2006.03.056 . PMID   16597440. S2CID   21490164.
  42. ↑ Tamura T, Sone M, Nakamura Y, Shimamura T, Imoto S, Miyano S, Okazawa H (January 2013). "A restricted level of PQBP1 is needed for the best longevity of Drosophila". Neurobiology of Aging. 34 (1): 356.e11–356.e20. doi:10.1016/j.neurobiolaging.2012.07.015. PMID   22901698. S2CID   17527056.

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