scholarly journals BIR Domain

2020 ◽  
Author(s):  
Keyword(s):  
Bir Domain

scholarly journals Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP

2004 ◽  
Vol 385 (1) ◽  
pp. 11-20 ◽  
Author(s):  
Domagoj VUCIC ◽  
Matthew C. FRANKLIN ◽  
Heidi J. A. WALLWEBER ◽  
Kanad DAS ◽  
Brendan P. ECKELMAN ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Caspase 9 ◽  
Direct Inhibition ◽  
The Third ◽  
Apoptotic Protein ◽  
Iap Antagonist ◽  
Repeat Domain ◽  
Apoptotic Activity ◽  
Bir Domain ◽  
Better Than

ML-IAP (melanoma inhibitor of apoptosis) is a potent anti-apoptotic protein that is strongly up-regulated in melanoma and confers protection against a variety of pro-apoptotic stimuli. The mechanism by which ML-IAP regulates apoptosis is unclear, although weak inhibition of caspases 3 and 9 has been reported. Here, the binding to and inhibition of caspase 9 by the single BIR (baculovirus IAP repeat) domain of ML-IAP has been investigated and found to be significantly less potent than the ubiquitously expressed XIAP (X-linked IAP). Engineering of the ML-IAP-BIR domain, based on comparisons with the third BIR domain of XIAP, resulted in a chimeric BIR domain that binds to and inhibits caspase 9 significantly better than either ML-IAP-BIR or XIAP-BIR3. Mutational analysis of the ML-IAP-BIR domain demonstrated that similar enhancements in caspase 9 affinity can be achieved with only three amino acid substitutions. However, none of these modifications affected binding of the ML-IAP-BIR domain to the IAP antagonist Smac (second mitochondrial activator of caspases). ML-IAP-BIR was found to bind mature Smac with low nanomolar affinity, similar to that of XIAP-BIR2-BIR3. Correspondingly, increased expression of ML-IAP results in formation of a ML-IAP–Smac complex and disruption of the endogenous interaction between XIAP and mature Smac. These results suggest that ML-IAP might regulate apoptosis by sequestering Smac and preventing it from antagonizing XIAP-mediated inhibition of caspases, rather than by direct inhibition of caspases.

The evolution of BIR domain and its containing proteins

FEBS Letters ◽  
2008 ◽  
Vol 582 (27) ◽  
pp. 3817-3822 ◽  
Author(s):  
Lihuan Cao ◽  
Zhenghan Wang ◽  
Xianmei Yang ◽  
Li Xie ◽  
Long Yu
Keyword(s):  
Bir Domain

325 CELF2 Induced Splicing Results in Loss of the Bir Domain in Survivin: Critical Role of XIAP in Radiation Induced Mitotic Catastrophe

2012 ◽  
Vol 142 (5) ◽  
pp. S-75
Author(s):  
David Standing ◽  
Prabhu Ramamoorthy ◽  
Parthasarathy Rangarajan ◽  
Dharmalingam Subramaniam ◽  
Satish Ramalingam ◽  
...  
Keyword(s):  
Critical Role ◽  
Mitotic Catastrophe ◽  
Radiation Induced ◽  
Bir Domain

scholarly journals Recognition of Smac-mimetic compounds by the BIR domain of cIAP1

2010 ◽  
Vol 19 (12) ◽  
pp. 2418-2429 ◽  
Author(s):  
Federica Cossu ◽  
Francesca Malvezzi ◽  
Giulia Canevari ◽  
Eloise Mastrangelo ◽  
Daniele Lecis ◽  
...  
Keyword(s):  
Smac Mimetic ◽  
Bir Domain

scholarly journals Molecular convergence by differential domain acquisition is a hallmark of chromosomal passenger complex evolution

2022 ◽  
Author(s):  
Shinichiro Komaki ◽  
Eelco C Tromer ◽  
Geert De Jaeger ◽  
Nancy De Winne ◽  
Maren Heese ◽  
...  
Keyword(s):  
Common Ancestor ◽  
Eukaryotic Cell ◽  
Binding Domain ◽  
Phosphate Binding ◽  
Fha Domain ◽  
Developmental Defects ◽  
Chromosomal Passenger Complex ◽  
Chromosomal Passenger ◽  
Similarity Searches ◽  
Bir Domain

The chromosomal passenger complex (CPC) is a heterotetrameric regulator of eukaryotic cell division, consisting of an Aurora-type kinase and a scaffold built of INCENP, Borealin and Survivin. While most CPC components are conserved across eukaryotes, orthologs of the chromatin reader Survivin have previously only been found in animals and fungi, raising the question of how its essential role is carried out in other eukaryotes. By characterizing proteins that bind to the Arabidopsis Borealin ortholog, we identified BOREALIN RELATED INTERACTOR 1 and 2 (BORI1 and BORI2) as redundant Survivin-like proteins in the context of the CPC in plants. Loss of BORI function is lethal and a reduced expression of BORIs causes severe developmental defects. Similar to Survivin, we find that the BORIs bind to phosphorylated histone H3, relevant for correct CPC association with chromatin. However, this interaction is not mediated by a BIR domain as in previously recognized Survivin orthologs, but by an FHA domain, a widely conserved phosphate-binding module. We propose that the unifying criterion of Survivin-type proteins is a helix that facilitates complex formation with the other two scaffold components, and that the addition of a phosphate-binding domain, necessary for concentration at the inner centromere, evolved in parallel in different eukaryotic groups. Using sensitive similarity searches, we indeed find conservation of this helical domain between animals and plants, and identify the missing CPC component in most eukaryotic supergroups. Interestingly, we also detect Survivin orthologs without a defined phosphate-binding domain, possibly reflecting the situation in the last eukaryotic common ancestor.

scholarly journals Third BIR domain of XIAP binds to both Cu(II) and Cu(I) in multiple sites and with diverse affinities characterized at atomic resolution

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Shen-Na Chen ◽  
Tian Fang ◽  
Jing-Yang Kong ◽  
Bin-Bin Pan ◽  
Xun-Cheng Su
Keyword(s):  
Atomic Resolution ◽  
Bir Domain

scholarly journals Role of Melanoma Inhibitor of Apoptosis (ML-IAP) Protein, a Member of the Baculoviral IAP Repeat (BIR) Domain Family, in the Regulation of C-RAF Kinase and Cell Migration

2012 ◽  
Vol 287 (34) ◽  
pp. 28445-28455 ◽  
Author(s):  
Tripat Kaur Oberoi-Khanuja ◽  
Christiaan Karreman ◽  
Sarit Larisch ◽  
Ulf R. Rapp ◽  
Krishnaraj Rajalingam
Keyword(s):  
Cell Migration ◽  
Protein A ◽  
Inhibitor Of Apoptosis ◽  
Domain Family ◽  
Raf Kinase ◽  
Bir Domain
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