XIAP

Last updated
XIAP
Protein BIRC4 PDB 1c9q.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases XIAP , API3, BIRC4, IAP-3, ILP1, MIHA, XLP2, hIAP-3, hIAP3, X-linked inhibitor of apoptosis
External IDs OMIM: 300079 MGI: 107572 HomoloGene: 901 GeneCards: XIAP
Orthologs
SpeciesHumanMouse
Entrez

331

11798

Ensembl

ENSG00000101966

ENSMUSG00000025860

UniProt

P98170

Q60989

RefSeq (mRNA)

NM_001167
NM_001204401

NM_001301639
NM_001301641
NM_009688

RefSeq (protein)

NP_001158
NP_001191330
NP_001365519
NP_001365520
NP_001365521

NP_001288568
NP_001288570
NP_033818

Location (UCSC)n/a Chr X: 41.15 – 41.2 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

X-linked inhibitor of apoptosis protein (XIAP), also known as inhibitor of apoptosis protein 3 (IAP3) and baculoviral IAP repeat-containing protein 4 (BIRC4), is a protein that stops apoptotic cell death. In humans, this protein (XIAP) is produced by a gene named XIAP gene located on the X chromosome. [4] [5]

XIAP is a member of the inhibitor of apoptosis family of proteins (IAP). IAPs were initially identified in baculoviruses, but XIAP is one of the homologous proteins found in mammals. [6] It is so called because it was first discovered by a 273 base pair site on the X chromosome. [4] The protein is also called human IAP-like Protein (hILP), because it is not as well conserved as the human IAPS: hIAP-1 and hIAP-2. [4] [7] XIAP is the most potent human IAP protein currently identified. [8]

Discovery

Neuronal apoptosis inhibitor protein (NAIP) was the first homolog to baculoviral IAPs that was identified in humans. [4] With the sequencing data of NIAP, the gene sequence for a RING zinc-finger domain was discovered at site Xq24-25. [4] Using PCR and cloning, three BIR domains and a RING finger were found on the protein, which became known as X-linked Inhibitor of Apoptosis Protein. The transcript size of Xiap is 9.0kb, with an open reading frame of 1.8kb. [4] Xiap mRNA has been observed in all human adult and fetal tissues "except peripheral blood leukocytes". [4] The XIAP sequences led to the discovery of other members of the IAP family.

Structure

XIAP consists of three major types of structural elements (domains). Firstly, there is the baculoviral IAP repeat (BIR) domain consisting of approximately 70 amino acids, which characterizes all IAP. [8] Secondly, there is a UBA domain, which allows XIAP to bind to ubiquitin. Thirdly, there is a zinc-binding domain, or a "carboxy-terminal RING Finger". [7] XIAP has been characterized with three amino-terminal BIR domains followed by one UBA domain and finally one RING domain. [9] Between the BIR-1 and BIR-2 domains, there is a linker-BIR-2 region that is thought to contain the only element that comes into contact with the caspase molecule to form the XIAP/Caspase-7 complex. [10] In solution the full length form of XIAP forms a homodimer of approximately 114 kDa. [11]

Function

XIAP stops apoptotic cell death that is induced either by viral infection or by overproduction of caspases. Caspases are the enzymes primarily responsible for cell death. [7] XIAP binds to and inhibits caspase 3, 7 and 9. [12] The BIR2 domain of XIAP inhibits caspase 3 and 7, while BIR3 binds to and inhibits caspase 9. [8] The RING domain utilizes E3 ubiquitin ligase activity and enables IAPs to catalyze ubiquination of self, caspase-3, or caspase-7 by degradation via proteasome activity. [13] However, mutations affecting the RING Finger do not significantly affect apoptosis, indicating that the BIR domain is sufficient for the protein's function. [7] When inhibiting caspase-3 and caspase-7 activity, the BIR2 domain of XIAP binds to the active-site substrate groove, blocking access of the normal protein substrate that would result in apoptosis. [13] [14]

Caspases are activated by cytochrome c, which is released into the cytosol by dysfunctioning mitochondria. [7] Studies show that XIAP does not directly affect cytochrome c. [7]

XIAP distinguishes itself from the other human IAPs because it is able to effectively prevent cell death due to "TNF-α, Fas, UV light, and genotoxic agents". [7]


Inhibiting XIAP

XIAP is inhibited by DIABLO (Smac) and HTRA2 (Omi), two death-signaling proteins released into the cytoplasm by the mitochondria. [9] Smac/DIABLO, a mitochondrial protein and negative regulator of XIAP, can enhance apoptosis by binding to XIAP and preventing it from binding to caspases. This allows normal caspase activity to proceed. The binding process of Smac/DIABLO to XIAP and caspase release requires a conserved tetrapeptide motif. [13]

Clinical significance

Deregulation of XIAP can result in "cancer, neurodegenerative disorders, and autoimmunity". [9] High proportions of XIAP may function as a tumor marker. [8] In the development of lung cancer NCI-H460, the overexpression of XIAP not only inhibits caspase, but also stops the activity of cytochrome c (Apoptosis). In developing prostate cancer, XIAP is one of four IAPs overexpressed in the prostatic epithelium, indicating that a molecule that inhibits all IAPs may be necessary for effective treatment. [15] Apoptotic regulation is an extremely important biological function, as evidenced by "the conservation of the IAPs from humans to Drosophila". [4]

Mutations in the XIAP gene can result in a severe and rare type of inflammatory bowel disease. [16] Defects in the XIAP gene can also result in an extremely rare condition called X-linked lymphoproliferative disease type 2. [16] [17] [18]

Interactions

XIAP has been shown to interact with:

Related Research Articles

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References

  1. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025860 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  5. ↑ Duckett CS, Nava VE, Gedrich RW, Clem RJ, Van Dongen JL, Gilfillan MC, Shiels H, Hardwick JM, Thompson CB (June 1996). "A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors". The EMBO Journal. 15 (11): 2685–94. doi:10.1002/j.1460-2075.1996.tb00629.x. PMC   450204 . PMID   8654366.
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  11. ↑ Polykretis P, Luchinat E, Bonucci A, Giachetti A, Graewert MA, Svergun DI, Banci L (September 2019). "Conformational characterization of full-length X-chromosome-linked inhibitor of apoptosis protein (XIAP) through an integrated approach". IUCrJ. 6 (Pt 5): 948–957. doi:10.1107/S205225251901073X. PMC   6760453 . PMID   31576227.
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  19. 1 2 Sanna MG, da Silva Correia J, Luo Y, Chuang B, Paulson LM, Nguyen B, Deveraux QL, Ulevitch RJ (August 2002). "ILPIP, a novel anti-apoptotic protein that enhances XIAP-mediated activation of JNK1 and protection against apoptosis". The Journal of Biological Chemistry. 277 (34): 30454–62. doi: 10.1074/jbc.M203312200 . PMID   12048196.
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  21. 1 2 Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (December 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". The EMBO Journal. 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. PMC   1170295 . PMID   9384571.
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  26. 1 2 Davoodi J, Lin L, Kelly J, Liston P, MacKenzie AE (September 2004). "Neuronal apoptosis-inhibitory protein does not interact with Smac and requires ATP to bind caspase-9". The Journal of Biological Chemistry. 279 (39): 40622–8. doi: 10.1074/jbc.M405963200 . PMID   15280366.
  27. ↑ Deveraux QL, Roy N, Stennicke HR, Van Arsdale T, Zhou Q, Srinivasula SM, Alnemri ES, Salvesen GS, Reed JC (April 1998). "IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases". The EMBO Journal. 17 (8): 2215–23. doi:10.1093/emboj/17.8.2215. PMC   1170566 . PMID   9545235.
  28. ↑ Richter BW, Mir SS, Eiben LJ, Lewis J, Reffey SB, Frattini A, Tian L, Frank S, Youle RJ, Nelson DL, Notarangelo LD, Vezzoni P, Fearnhead HO, Duckett CS (July 2001). "Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis protein family". Molecular and Cellular Biology. 21 (13): 4292–301. doi:10.1128/MCB.21.13.4292-4301.2001. PMC   87089 . PMID   11390657.
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  32. ↑ Verhagen AM, Ekert PG, Pakusch M, Silke J, Connolly LM, Reid GE, Moritz RL, Simpson RJ, Vaux DL (July 2000). "Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins". Cell. 102 (1): 43–53. doi: 10.1016/S0092-8674(00)00009-X . PMID   10929712. S2CID   3192775.
  33. ↑ Hegde R, Srinivasula SM, Datta P, Madesh M, Wassell R, Zhang Z, Cheong N, Nejmeh J, Fernandes-Alnemri T, Hoshino S, Alnemri ES (October 2003). "The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein". The Journal of Biological Chemistry. 278 (40): 38699–706. doi: 10.1074/jbc.M303179200 . PMID   12865429.
  34. ↑ Jordan BW, Dinev D, LeMellay V, Troppmair J, Gotz R, Wixler L, Sendtner M, Ludwig S, Rapp UR (October 2001). "Neurotrophin receptor-interacting mage homologue is an inducible inhibitor of apoptosis protein-interacting protein that augments cell death". The Journal of Biological Chemistry. 276 (43): 39985–9. doi: 10.1074/jbc.C100171200 . PMID   11546791.
  35. ↑ Winsauer G, Resch U, Hofer-Warbinek R, Schichl YM, de Martin R (November 2008). "XIAP regulates bi-phasic NF-kappaB induction involving physical interaction and ubiquitination of MEKK2". Cellular Signalling. 20 (11): 2107–12. doi:10.1016/j.cellsig.2008.08.004. PMID   18761086.
  36. ↑ Yamaguchi K, Nagai S, Ninomiya-Tsuji J, Nishita M, Tamai K, Irie K, Ueno N, Nishida E, Shibuya H, Matsumoto K (January 1999). "XIAP, a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway". The EMBO Journal. 18 (1): 179–87. doi:10.1093/emboj/18.1.179. PMC   1171113 . PMID   9878061.
  37. ↑ Liston P, Fong WG, Kelly NL, Toji S, Miyazaki T, Conte D, Tamai K, Craig CG, McBurney MW, Korneluk RG (February 2001). "Identification of XAF1 as an antagonist of XIAP anti-Caspase activity". Nature Cell Biology. 3 (2): 128–33. doi:10.1038/35055027. PMID   11175744. S2CID   19731886.

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