AH receptor-interacting protein

Aryl hydrocarbon receptor interacting protein
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsAIP ; ARA9; FKBP16; FKBP37; SMTPHN; XAP-2; XAP2
External IDsOMIM: 605555 MGI: 109622 HomoloGene: 2959 GeneCards: AIP Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez904911632
EnsemblENSG00000110711ENSMUSG00000024847
UniProtO00170O08915
RefSeq (mRNA)NM_003977NM_001276284
RefSeq (protein)NP_003968NP_001263213
Location (UCSC)Chr 11:
67.25 – 67.26 Mb
Chr 19:
4.11 – 4.13 Mb
PubMed search

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]

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]

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.[4]

Interactions

AIP has been shown to interact with the aryl hydrocarbon receptor,[3][5][6] peroxisome proliferator-activated receptor alpha[7] and the aryl hydrocarbon receptor nuclear translocator.[3][8]

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. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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