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
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. [39] 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. [40] [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. [40] 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. [41] [42] The hypomorph Drosophila model revealed molecular function of PQBP1 in learning acquisition mediated by decreased mRNA and protein expressions of NMDA receptor subunit NR1. [41] Research indicates that in order to appropriately function, the protein must be expressed within a critical range. [43] [10]

Related Research Articles

<span class="mw-page-title-main">Alternative splicing</span> Process by which a gene can code for multiple proteins

Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. In this process, particular exons of a gene may be included within or excluded from the final, processed messenger RNA (mRNA) produced from that gene. This means the exons are joined in different combinations, leading to different (alternative) mRNA strands. Consequently, the proteins translated from alternatively spliced mRNAs usually contain differences in their amino acid sequence and, often, in their biological functions.

<span class="mw-page-title-main">L1 (protein)</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">FMR1</span> Human protein and coding gene

FMR1 is a human gene that codes for a protein called fragile X messenger ribonucleoprotein, or FMRP. This protein, most commonly found in the brain, is essential for normal cognitive development and female reproductive function. Mutations of this gene can lead to fragile X syndrome, intellectual disability, premature ovarian failure, autism, Parkinson's disease, developmental delays and other cognitive deficits. The FMR1 premutation is associated with a wide spectrum of clinical phenotypes that affect more than two million people worldwide.

IKBKAP is a human gene encoding the IKAP protein, which is ubiquitously expressed at varying levels in all tissue types, including brain cells. The IKAP protein is thought to participate as a sub-unit in the assembly of a six-protein putative human holo-Elongator complex, which allows for transcriptional elongation by RNA polymerase II. Further evidence has implicated the IKAP protein as being critical in neuronal development, and directs that decreased expression of IKAP in certain cell types is the molecular basis for the severe, neurodevelopmental disorder familial dysautonomia. Other pathways that have been connected to IKAP protein function in a variety of organisms include tRNA modification, cell motility, and cytosolic stress signalling. Homologs of the IKBKAP gene have been identified in multiple other Eukaryotic model organisms. Notable homologs include Elp1 in yeast, Ikbkap in mice, and D-elp1 in fruit flies. The fruit fly homolog (D-elp1) has RNA-dependent RNA polymerase activity and is involved in RNA interference.

<span class="mw-page-title-main">PAX3</span> Paired box gene 3

The PAX3 gene encodes a member of the paired box or PAX family of transcription factors. The PAX family consists of nine human (PAX1-PAX9) and nine mouse (Pax1-Pax9) members arranged into four subfamilies. Human PAX3 and mouse Pax3 are present in a subfamily along with the highly homologous human PAX7 and mouse Pax7 genes. The human PAX3 gene is located in the 2q36.1 chromosomal region, and contains 10 exons within a 100 kb region.

Prickle is also known as REST/NRSF-interacting LIM domain protein, which is a putative nuclear translocation receptor. Prickle is part of the non-canonical Wnt signaling pathway that establishes planar cell polarity. A gain or loss of function of Prickle1 causes defects in the convergent extension movements of gastrulation. In epithelial cells, Prickle2 establishes and maintains cell apical/basal polarity. Prickle1 plays an important role in the development of the nervous system by regulating the movement of nerve cells.

<span class="mw-page-title-main">Ataxin 1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Collagen, type III, alpha 1</span>

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<span class="mw-page-title-main">TP63</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">HNRNPK</span> Human protein and coding gene

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<span class="mw-page-title-main">USH1C</span>

Harmonin is a protein that in humans is encoded by the USH1C gene. It is expressed in sensory cells of the inner ear and retina, where it plays a role in hearing, balance, and vision. Mutations at the USH1C locus cause Usher syndrome type 1c and nonsyndromic sensorineural deafness.

<span class="mw-page-title-main">Retinitis pigmentosa GTPase regulator</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">SON (gene)</span> Protein-coding gene in the species Homo sapiens

SON protein is a protein that in humans is encoded by the SON gene.

<span class="mw-page-title-main">ERN1</span> Protein-coding gene in the species Homo sapiens

The serine/threonine-protein kinase/endoribonuclease inositol-requiring enzyme 1 α (IRE1α) is an enzyme that in humans is encoded by the ERN1 gene.

<span class="mw-page-title-main">TBX3</span> Protein-coding gene in the species Homo sapiens

T-box transcription factor TBX3 is a protein that in humans is encoded by the TBX3 gene.

<span class="mw-page-title-main">POU3F2</span> Protein-coding gene in the species Homo sapiens

POU domain, class 3, transcription factor 2 is a protein that in humans is encoded by the POU3F2 gene.

<span class="mw-page-title-main">RBM10</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">TXNL4A</span> Protein-coding gene in the species Homo sapiens

Thioredoxin-like protein 4A is a protein that is encoded by the TXNL4A gene in humans.

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<span class="mw-page-title-main">Renpenning's syndrome</span> Medical condition

Renpenning's syndrome is a neurodevelopmental disorder recognised in males that causes intellectual disability, mild growth retardation with examples in the testes and head, and a somewhat short stature. The condition only affects males, starting at birth.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000102103 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031157 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 Imafuku I, Waragai M, Takeuchi S, Kanazawa I, Kawabata M, Mouradian MM, Okazawa H (December 1998). "Polar amino acid-rich sequences bind to polyglutamine tracts". Biochemical and Biophysical Research Communications. 253 (1): 16–20. doi:10.1006/bbrc.1998.9725. PMID   9875212.
  6. ↑ Lenski C, Abidi F, Meindl A, Gibson A, Platzer M, Frank Kooy R, et al. (April 2004). "Novel truncating mutations in the polyglutamine tract binding protein 1 gene (PQBP1) cause Renpenning syndrome and X-linked mental retardation in another family with microcephaly". American Journal of Human Genetics. 74 (4): 777–780. doi:10.1086/383205. PMC   1181956 . PMID   15024694.
  7. 1 2 3 4 5 Waragai M, Lammers CH, Takeuchi S, Imafuku I, Udagawa Y, Kanazawa I, et al. (June 1999). "PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival". Human Molecular Genetics. 8 (6): 977–987. doi: 10.1093/hmg/8.6.977 . PMID   10332029.
  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.
  9. ↑ Qi Y, Hoshino M, Wada Y, Marubuchi S, Yoshimura N, Kanazawa I, et al. (September 2005). "PQBP-1 is expressed predominantly in the central nervous system during development". The European Journal of Neuroscience. 22 (6): 1277–1286. doi:10.1111/j.1460-9568.2005.04339.x. PMID   16190883. S2CID   33492223.
  10. 1 2 3 Iwasaki Y, Thomsen GH (October 2014). "The splicing factor PQBP1 regulates mesodermal and neural development through FGF signaling". Development. 141 (19): 3740–3751. doi:10.1242/dev.106658. PMC   4197583 . PMID   25209246.
  11. 1 2 3 Okazawa H, Rich T, Chang A, Lin X, Waragai M, Kajikawa M, et al. (May 2002). "Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death". Neuron. 34 (5): 701–713. doi: 10.1016/S0896-6273(02)00697-9 . PMID   12062018. S2CID   17652186.
  12. 1 2 3 Jin M, Shiwaku H, Tanaka H, Obita T, Ohuchi S, Yoshioka Y, et al. (November 2021). "Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation". Nature Communications. 12 (1): 6565. Bibcode:2021NatCo..12.6565J. doi:10.1038/s41467-021-26851-2. PMC   8592984 . PMID   34782623.
  13. ↑ Kunde SA, Musante L, Grimme A, Fischer U, Müller E, Wanker EE, Kalscheuer VM (December 2011). "The X-chromosome-linked intellectual disability protein PQBP1 is a component of neuronal RNA granules and regulates the appearance of stress granules". Human Molecular Genetics. 20 (24): 4916–4931. doi: 10.1093/hmg/ddr430 . PMID   21933836.
  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".
  16. 1 2 3 Ito H, Shiwaku H, Yoshida C, Homma H, Luo H, Chen X, et al. (April 2015). "In utero gene therapy rescues microcephaly caused by Pqbp1-hypofunction in neural stem progenitor cells". Molecular Psychiatry. 20 (4): 459–471. doi:10.1038/mp.2014.69. PMC   4378255 . PMID   25070536.
  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.
  21. ↑ 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 (1): 3822. Bibcode:2014NatCo...5.3822M. doi: 10.1038/ncomms4822 . PMID   24781215.
  22. ↑ Wang Q, Moore MJ, Adelmant G, Marto JA, Silver PA (March 2013). "PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth". Genes & Development. 27 (6): 615–626. doi:10.1101/gad.212308.112. PMC   3613609 . PMID   23512658.
  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.
  25. ↑ Musante L, Kunde SA, Sulistio TO, Fischer U, Grimme A, Frints SG, et al. (January 2010). "Common pathological mutations in PQBP1 induce nonsense-mediated mRNA decay and enhance exclusion of the mutant exon". Human Mutation. 31 (1): 90–98. doi: 10.1002/humu.21146 . PMID   19847789. S2CID   23152883.
  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. ↑ 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.
  28. 1 2 Stevenson RE, Bennett CW, Abidi F, Kleefstra T, Porteous M, Simensen RJ, et al. (May 2005). "Renpenning syndrome comes into focus". American Journal of Medical Genetics. Part A. 134 (4): 415–421. doi:10.1002/ajmg.a.30664. PMID   15782410. S2CID   24333408.
  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.
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  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. ↑ 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.
  40. 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.
  41. 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.
  42. ↑ 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.
  43. ↑ 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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