AH receptor-interacting protein: Difference between revisions

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== Function ==
== Function ==


AIP may play a positive role in [[aryl hydrocarbon receptor]]-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the [[hepatitis B virus]] (HBV) X protein.<ref name="entrez"/>
AIP may play a positive role in [[aryl hydrocarbon receptor]]-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the [[hepatitis B virus]] (HBV) X protein.<ref name="entrez"/> Further, it's been known to suppress antiviral signaling and the induction of type I interferon by targeting IRF7, a key player in the antiviral signal pathways.<ref name = "Zhou_2005">{{cite journal | vauthors = Zhou Q, Lavorgna A, Bowman M, Hiscott J, Harhaj EW | title = Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon | journal = The Journal of Biological Chemistry | volume = 290 | issue = 23 | pages = 14729–39 | date = June 2015 | pmid = 25911105 | doi = 10.1074/jbc.M114.633065 | pmc = 4505538 }}</ref>


== Role in disease ==
== Role in disease ==


AIP mutations may be the cause of a familial form of [[acromegaly]], familial isolated pituitary adenoma (FIPA). Somatotropinomas (i.e. [[Growth hormone|GH]]-producing [[pituitary adenoma]]s), sometimes associated with [[prolactinoma]]s, are present in most AIP mutated patients.<ref name = "pmid20530095">{{cite journal | vauthors=Occhi G, Trivellin G, Ceccato F |title=Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia. |journal=Eur. J. Endocrinol. |year=2010 |volume=163 |issue=3 |pages=369–376 |doi=10.1530/EJE-10-0327 |pmid=20530095 |url=http://eje-online.org/content/163/3/369.long |display-authors=etal}}</ref>
AIP mutations may be the cause of a familial form of [[acromegaly]], familial isolated pituitary adenoma (FIPA). Somatotropinomas (i.e. [[Growth hormone|GH]]-producing [[pituitary adenoma]]s), sometimes associated with [[prolactinoma]]s, are present in most AIP mutated patients.<ref name="pmid20530095">{{cite journal |vauthors=Occhi G, Trivellin G, Ceccato F |title=Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia. |journal=Eur. J. Endocrinol. |year=2010 |volume=163 |issue=3 |pages=369–376 |doi=10.1530/EJE-10-0327 |pmid=20530095 |url=http://eje-online.org/content/163/3/369.long |display-authors=etal |access-date=2012-03-22 |archive-url=https://archive.is/20130414175732/http://eje-online.org/content/163/3/369.long |archive-date=2013-04-14 |dead-url=yes |df= }}</ref>


== Interactions ==
== Interactions ==


AIP has been shown to [[Protein-protein interaction|interact]] with the [[aryl hydrocarbon receptor]],<ref name = "pmid9111057"/><ref name="pmid10986286">{{cite journal | vauthors = Petrulis JR, Hord NG, Perdew GH | title = Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2 | journal = J. Biol. Chem. | volume = 275 | issue = 48 | pages = 37448–53 |date=December 2000 | pmid = 10986286 | doi = 10.1074/jbc.M006873200 | url = | issn = }}</ref><ref name="pmid9083006">{{cite journal | vauthors = Ma Q, Whitlock JP | title = A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin | journal = J. Biol. Chem. | volume = 272 | issue = 14 | pages = 8878–84 |date=April 1997 | pmid = 9083006 | doi = 10.1074/jbc.272.14.8878| url = | issn = }}</ref> [[peroxisome proliferator-activated receptor alpha]]<ref name="pmid12482853">{{cite journal | vauthors = Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH | title = Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2 | journal = J. Biol. Chem. | volume = 278 | issue = 7 | pages = 4467–73 |date=February 2003 | pmid = 12482853 | doi = 10.1074/jbc.M211261200 | url = | issn = }}</ref> and the [[aryl hydrocarbon receptor nuclear translocator]].<ref name=pmid9111057/><ref name="pmid11259606">{{cite journal | vauthors = Kazlauskas A, Sundström S, Poellinger L, Pongratz I | title = The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor | journal = Mol. Cell. Biol. | volume = 21 | issue = 7 | pages = 2594–607 |date=April 2001 | pmid = 11259606 | pmc = 86890 | doi = 10.1128/MCB.21.7.2594-2607.2001 | url = | issn = }}</ref>
AIP has been shown to [[Protein-protein interaction|interact]] with the [[aryl hydrocarbon receptor]],<ref name = "pmid9111057"/><ref name="pmid10986286">{{cite journal | vauthors = Petrulis JR, Hord NG, Perdew GH | title = Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2 | journal = J. Biol. Chem. | volume = 275 | issue = 48 | pages = 37448–53 |date=December 2000 | pmid = 10986286 | doi = 10.1074/jbc.M006873200 | url = | issn = }}</ref><ref name="pmid9083006">{{cite journal | vauthors = Ma Q, Whitlock JP | title = A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin | journal = J. Biol. Chem. | volume = 272 | issue = 14 | pages = 8878–84 |date=April 1997 | pmid = 9083006 | doi = 10.1074/jbc.272.14.8878| url = | issn = }}</ref> [[peroxisome proliferator-activated receptor alpha]]<ref name="pmid12482853">{{cite journal | vauthors = Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH | title = Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2 | journal = J. Biol. Chem. | volume = 278 | issue = 7 | pages = 4467–73 |date=February 2003 | pmid = 12482853 | doi = 10.1074/jbc.M211261200 | url = | issn = }}</ref> and the [[aryl hydrocarbon receptor nuclear translocator]].<ref name=pmid9111057/><ref name="pmid11259606">{{cite journal | vauthors = Kazlauskas A, Sundström S, Poellinger L, Pongratz I | title = The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor | journal = Mol. Cell. Biol. | volume = 21 | issue = 7 | pages = 2594–607 |date=April 2001 | pmid = 11259606 | pmc = 86890 | doi = 10.1128/MCB.21.7.2594-2607.2001 | url = | issn = }}</ref> Further, it has shown that AIP can interact with IRF7 to exert its novel function of negatively regulating antiviral signal pathways.<ref name = "Zhou_2005" />


==References==
==References==
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==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin|2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | vauthors=Zhou Q, Lavorgna A |title=Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon. |journal=Journal of Biological Chemistry |year=2015 |volume=290 |pages=14729–14739 |doi=10.1074/jbc.M114.633065 |url=http://www.jbc.org/content/290/23/14729.short |display-authors=etal|pmc=4505538 }}
*{{cite journal  | vauthors=Chen HS, Perdew GH |title=Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27554–8 |year= 1994 |pmid= 7961671 |doi=  }}
*{{cite journal  | vauthors=Chen HS, Perdew GH |title=Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27554–8 |year= 1994 |pmid= 7961671 |doi=  }}
*{{cite journal  | vauthors=Ma Q, Whitlock JP |title=A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 8878–84 |year= 1997 |pmid= 9083006 |doi=10.1074/jbc.272.14.8878  }}
*{{cite journal  | vauthors=Ma Q, Whitlock JP |title=A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 8878–84 |year= 1997 |pmid= 9083006 |doi=10.1074/jbc.272.14.8878  }}
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*{{cite journal  | vauthors=Yano M, Terada K, Mori M |title=AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins. |journal=J. Cell Biol. |volume=163 |issue= 1 |pages= 45–56 |year= 2003 |pmid= 14557246  | pmc=2173431 |doi= 10.1083/jcb.200305051 }}
*{{cite journal  | vauthors=Yano M, Terada K, Mori M |title=AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins. |journal=J. Cell Biol. |volume=163 |issue= 1 |pages= 45–56 |year= 2003 |pmid= 14557246  | pmc=2173431 |doi= 10.1083/jcb.200305051 }}
*{{cite journal  | vauthors=Ramadoss P, Petrulis JR, Hollingshead BD |title=Divergent roles of hepatitis B virus X-associated protein 2 (XAP2) in human versus mouse Ah receptor complexes. |journal=Biochemistry |volume=43 |issue= 3 |pages= 700–9 |year= 2004 |pmid= 14730974 |doi= 10.1021/bi035827v |display-authors=etal}}
*{{cite journal  | vauthors=Ramadoss P, Petrulis JR, Hollingshead BD |title=Divergent roles of hepatitis B virus X-associated protein 2 (XAP2) in human versus mouse Ah receptor complexes. |journal=Biochemistry |volume=43 |issue= 3 |pages= 700–9 |year= 2004 |pmid= 14730974 |doi= 10.1021/bi035827v |display-authors=etal}}
*{{cite journal | vauthors=Occhi G, Trivellin G, Ceccato F |title=Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia. |journal=Eur. J. Endocrinol. |year=2010 |volume=163 |issue=3 |pages=369–376 |doi=10.1530/EJE-10-0327 |pmid=20530095 |url=http://eje-online.org/content/163/3/369.long |display-authors=etal}}
*{{cite journal |vauthors=Occhi G, Trivellin G, Ceccato F |title=Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia. |journal=Eur. J. Endocrinol. |year=2010 |volume=163 |issue=3 |pages=369–376 |doi=10.1530/EJE-10-0327 |pmid=20530095 |url=http://eje-online.org/content/163/3/369.long |display-authors=etal |access-date=2012-03-22 |archive-url=https://archive.is/20130414175732/http://eje-online.org/content/163/3/369.long |archive-date=2013-04-14 |dead-url=yes |df= }}
}}
}}
{{refend}}
{{refend}}

Latest revision as of 03:15, 28 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

AH receptor-interacting protein (AIP) also known as aryl-hydrocarbon receptor-interacting protein, immunophilin homolog ARA9, or HBV X-associated protein 2 (XAP-2) is a protein that in humans is encoded by the AIP gene.[1][2][3] The protein is a member of FKBP family.

Function

AIP may play a positive role in aryl hydrocarbon receptor-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the hepatitis B virus (HBV) X protein.[1] Further, it's been known to suppress antiviral signaling and the induction of type I interferon by targeting IRF7, a key player in the antiviral signal pathways.[4]

Role in disease

AIP mutations may be the cause of a familial form of acromegaly, familial isolated pituitary adenoma (FIPA). Somatotropinomas (i.e. GH-producing pituitary adenomas), sometimes associated with prolactinomas, are present in most AIP mutated patients.[5]

Interactions

AIP has been shown to interact with the aryl hydrocarbon receptor,[3][6][7] peroxisome proliferator-activated receptor alpha[8] and the aryl hydrocarbon receptor nuclear translocator.[3][9] Further, it has shown that AIP can interact with IRF7 to exert its novel function of negatively regulating antiviral signal pathways.[4]

References

  1. 1.0 1.1 "Entrez Gene: AIP aryl hydrocarbon receptor interacting protein".
  2. Kuzhandaivelu N, Cong YS, Inouye C, Yang WM, Seto E (December 1996). "XAP2, a novel hepatitis B virus X-associated protein that inhibits X transactivation". Nucleic Acids Res. 24 (23): 4741–50. doi:10.1093/nar/24.23.4741. PMC 146319. PMID 8972861.
  3. 3.0 3.1 3.2 Carver LA, Bradfield CA (April 1997). "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo". J. Biol. Chem. 272 (17): 11452–6. doi:10.1074/jbc.272.17.11452. PMID 9111057.
  4. 4.0 4.1 Zhou Q, Lavorgna A, Bowman M, Hiscott J, Harhaj EW (June 2015). "Aryl Hydrocarbon Receptor Interacting Protein Targets IRF7 to Suppress Antiviral Signaling and the Induction of Type I Interferon". The Journal of Biological Chemistry. 290 (23): 14729–39. doi:10.1074/jbc.M114.633065. PMC 4505538. PMID 25911105.
  5. Occhi G, Trivellin G, Ceccato F, et al. (2010). "Prevalence of AIP mutations in a large series of sporadic Italian acromegalic patients and evaluation of CDKN1B status in acromegalic patients with multiple endocrine neoplasia". Eur. J. Endocrinol. 163 (3): 369–376. doi:10.1530/EJE-10-0327. PMID 20530095. Archived from the original on 2013-04-14. Retrieved 2012-03-22.
  6. Petrulis JR, Hord NG, Perdew GH (December 2000). "Subcellular localization of the aryl hydrocarbon receptor is modulated by the immunophilin homolog hepatitis B virus X-associated protein 2". J. Biol. Chem. 275 (48): 37448–53. doi:10.1074/jbc.M006873200. PMID 10986286.
  7. Ma Q, Whitlock JP (April 1997). "A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin". J. Biol. Chem. 272 (14): 8878–84. doi:10.1074/jbc.272.14.8878. PMID 9083006.
  8. Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH (February 2003). "Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2". J. Biol. Chem. 278 (7): 4467–73. doi:10.1074/jbc.M211261200. PMID 12482853.
  9. Kazlauskas A, Sundström S, Poellinger L, Pongratz I (April 2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. 21 (7): 2594–607. doi:10.1128/MCB.21.7.2594-2607.2001. PMC 86890. PMID 11259606.

Further reading