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Baculoviral IAP repeat-containing protein 5

Definition:

Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Essential for the maintenance of mitochondrial integrity and function. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.

References:

[1]. F Li, et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature. 1998 Dec 10;396(6711):580-4. [Content Brief]

[2]. S K Knauer, et al. An otoprotective role for the apoptosis inhibitor protein survivin. Cell Death Dis. 2010 Jul 1;1(7):e51. [Content Brief]

[3]. Fang Xia, et al. A survivin-ran complex regulates spindle formation in tumor cells. Mol Cell Biol. 2008 Sep;28(17):5299-311. [Content Brief]

[4]. Hiroyuki Marusawa, et al. HBXIP functions as a cofactor of survivin in apoptosis suppression. EMBO J. 2003 Jun 2;22(11):2729-40. [Content Brief]

[5]. Marat S Pavlyukov, et al. Survivin monomer plays an essential role in apoptosis regulation. J Biol Chem. 2011 Jul 1;286(26):23296-307. [Content Brief]

[6]. Queenie P Vong, et al. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science. 2005 Dec 2;310(5753):1499-504. [Content Brief]

[7]. Yuya Yamagishi, et al. Two histone marks establish the inner centromere and chromosome bi-orientation. Science. 2010 Oct 8;330(6001):239-43. [Content Brief]

[8]. Haijuan Wang, et al. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem. 2010 Nov 12;285(46):36129-37. [Content Brief]

[9]. Negusse Habtemichael, et al. Expression analysis suggests a potential cytoprotective role of Birc5 in the inner ear. Mol Cell Neurosci. 2010 Nov;45(3):297-305. [Content Brief]

[10]. M Kamran, et al. Aurora kinase A regulates Survivin stability through targeting FBXL7 in gastric cancer drug resistance and prognosis. Oncogenesis. 2017 Feb 20;6(2):e298. [Content Brief]

[11]. Elizabeth A Noton, et al. Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis. J Biol Chem. 2006 Jan 13;281(2):1286-95. [Content Brief]

[12]. C Mahotka, et al. Survivin-deltaEx3 and survivin-2B: two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties. Cancer Res. 1999 Dec 15;59(24):6097-102. [Content Brief]

[13]. Yuan Liu, et al. The Proapoptotic F-box Protein Fbxl7 Regulates Mitochondrial Function by Mediating the Ubiquitylation and Proteasomal Degradation of Survivin. J Biol Chem. 2015 May 8;290(19):11843-52. [Content Brief]

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