The isomerization of BRCA1 – BARD1 promotes the safety of replication forks
Zeman, M. Ok. & Cimprich, Ok. A. Causes and penalties of replication stress. Nat. Cell Biol. 16, 2-9 (2014).
Sidorova, J. A set of substrates: transforming of the replication fork and its roles in genome stability and chemoresistance. Cell Stress 1, 115-133 (2017).
Cantor, S.B. and Calvo, J. A. Fork safety and resistance to therapy of hereditary breast most cancers. Chilly Harb Spring. Symp. As. Biol. 82, 339-348 (2017).
Hashimoto, Y., Ray Chaudhuri, A., Lopes, M. & Costanzo, V. Rad51 defend the nascent DNA from Mre11-dependent degradation and promote the continual synthesis of DNA. Nat. Struct. Mol. Biol. 17, 1305-1311 (2010).
Schlacher, Ok. et al. Impartial function of double-strand break restore for BRCA2 in blocking the blocked degradation of the replication fork by MRE11. Cell 145, 529-542 (2011).
Zadorozhny, Ok. et al. The mutations related to Fanconi anemia destabilize the RAD51 filaments and compromise the safety of the replication fork. Cell Rep. 21, 333-340 (2017).
Wang, A. T. et al. A dominant mutation in human RAD51 reveals its perform within the restore of inter-band crosslinking of DNA, no matter homologous recombination. Mol. Cell 59, 478-490 (2015).
Ameziane, N. et al. A brand new subtype of Fanconi anemia related to a predominantly unfavorable mutation in RAD51. Nat. Widespread. 6, 8829 (2015).
Higgs, M.R. & Stewart, G.S. Safety or resection: BOD1L as a brand new protecting issue for the replication fork. Nucleus 7, 34-40 (2016).
Dungrawala, H. et al. RADX promotes genome stability and modulates chemosensitivity by regulating RAD51 on the replication forks. Mol. Cell 67, 374-386 (2017).
Bhat, Ok.P. et al. RADX modulates the exercise of RAD51 to manage the safety of the replication fork. Cell Rep. 24, 538-545 (2018).
Ray Chaudhuri, A. et al. The soundness of the replication fork confers chemoresistance to BRCA poor cells. Nature 535, 382-387 (2016).
Yazinski, S.A. et al. Inhibition of ATR disrupts the homologous recombination and fork safety pathways rewired in BRCA-deficient most cancers cells immune to the PARP inhibitor. Genes Dev. 31, 318-332 (2017).
Feng, W. and Jasin, M. BRCA2 suppress mitotic and G1 abnormalities induced by homologous recombination-related replication stress. Nat. Widespread. eight, 525 (2017).
Dungrawala, H. & Cortez, D. Purification of proteins on newly synthesized DNA utilizing iPOND. Mol. Biol. 1228, 123-131 (2015).
Sirbu, B.M. et al. Identification of proteins on energetic, blocked and collapsed replication forks utilizing protein isolation on nascent DNA (iPOND) coupled with mass spectrometry. J. Biol. Chem. 288, 31458-3177 (2013).
Schlacher, Ok., Wu, H. and Jasin, M. A separate replication fork safety tract connects tumor suppressors from Fanconi anemia to RAD51-BRCA1 / 2. Most cancers Cell 22, 106-116 (2012).
Zhang, F., Fan, Q., Ren, Ok., and Andreassen, P. R. PALB2 functionally hyperlink susceptibility proteins to BRCA1 and BRCA2 breast most cancers. Mol. Most cancers Res 7, 1110-1118 (2009).
Zhang, F. et al. PALB2 hyperlinks BRCA1 and BRCA2 within the response to DNA injury. Curr. Biol. 19, 524-529 (2009).
Sy, S.M., Huen, M.S. & Chen, J. PALB2 is a vital part of the BRCA complicated required for homologous recombination restore. Proc. Natl Acad. Sci. USA 106, 7155-7160 (2009).
Zhao, W. et al. BRCA1 – BARD1 promotes the pairing of homologous DNA by RAD51. Nature 550, 360-365 (2017).
Paull, T., D. Cortez, B. Bowers, Elledge, S.J. and Gellert, M. Direct Liaison to DNA by Brca1. Proc. Natl Acad. Sci. USA 98, 6086-6091 (2001).
Densham, R.M. et al. The exercise of BRCA1 – BARD1 human ubiquitin ligase neutralizes the limitations of chromatin throughout DNA resection. Nat. Struct. Mol. Biol. 23, 647-655 (2016).
Hayami, R. et al. Down regulation of BRCA1 – BARD1 ubiquitin ligase by CDK2. Most cancers Res. 65, 6-10 (2005).
Mertins, P. et al. Built-in proteomic evaluation of post-translational modifications by serial enrichment. Nat. Strategies 10, 634-637 (2013).
Steger, M. et al. Prolyl isomerase PIN1 regulates the restore of DNA double-strand breakage by neutralizing the ultimate resection of DNA. Mol. Cell 50, 333-343 (2013).
Zheng, H. et al. Pin1 prolyl isomerase is a regulator of the genotoxic response of p53. Nature 419, 849-853 (2002).
Nepomuceno, T. C. et al. Recruitment of BRCA1 into broken DNA websites relies on CDK9. Cell Cycle 16, 665-672 (2017).
Weiss, M.S., Jabs, A. and Hilgenfeld, R. Peptide hyperlinks revisited. Nat. Struct. Biol. 5, 676 (1998).
Alderson, T.R., Lee, J.H., Charlier, C., Ying, J. & Bax, A. Propensity for the formation of cis-proline in unfolded proteins. ChemBioChem 19, 37-42 (2018).
Göthel, S.F. & Marahiel, M.A. Peptidyl-prolyl-cis-trans-isomerases, a superfamily of ubiquitous refolding catalysts. Cell. Mol. Life Sci. 55, 423-436 (1999).
Ranganathan, R., Lu, Ok.P., Hunter, T. & Noel, J.P.The structural and useful evaluation of mitotic rotamase Pin1 means that substrate recognition relies on phosphorylation. Cell 89, 875-886 (1997).
Lu, Ok.P., Hanes, S.D. & Hunter, T. A human peptidyl-prolyl-isomerase important for the regulation of mitosis. Nature 380, 544-547 (1996).
Yaffe, M.B. et al. Sequence-specific and phosphorylation-dependent proline isomerization: potential mitotic regulation mechanism. Science 278, 1957-1960 (1997).
Lu, P.J., Zhou, X.Z., Shen, M. and Lu, Ok.P. Capabilities of WW domains as phosphoserine or phosphothreonine binding modules. Science 283, 1325-1328 (1999).
Nakamura, Ok. et al. Antibodies particular for proline isomers reveal the early conformation of tau protein in Alzheimer's illness. Cell 149, 232-244 (2012).
Hilton, B.A. et al. ATR performs a direct antiapoptotic function on the stage of the mitochondria, which is regulated by the prolyl isomerase Pin1. Mol. Cell 60, 35-46 (2015).
Zhou, X. Z. et al. Pin1-dependent prolyl isomerization regulates the dephosphorylation of Cdc25C and tau proteins. Mol. Cell 6, 873-883 (2000).
Innes, B.T., Bailey, M.L., Brandl, C.J., Shilton, B.H. and Litchfield, D.W. Non-catalytic participation of the Pin1 peptidylprolylisomerase area in goal binding. Entrance. Physiol. four, 18 (2013).
Taglialatela, A. et al. Restoration of replication fork stability in BRCA1 and BRCA2 poor cells by inactivation of SNF2 household fork remodelers. Mol. Cell 68, 414-430 (2017).
Petermann, E., Orta, ML, Issaeva, N., Schultz, N. and Helleday, T. Hydroxyurea-blocked replication forks step by step grow to be inactivated and require two totally different RAD51-mediated pathways for restarting and resuspending. restore. Mol. Cell 37, 492-502 (2010).
Hanada, Ok. et al. The Mus81-specific endonuclease assists in restarting replication by producing double-stranded DNA breaks. Nat. Struct. Mol. Biol. 14, 1096-1104 (2007).
Cerami, E. et al. The cBio most cancers genomics portal: an open platform for exploring multidimensional knowledge on most cancers genomics. Most cancers Discov. 2, 401-404 (2012).
Gao, J. et al. Integrative evaluation of complicated most cancers genomics and medical profiles utilizing cBioPortal. Sci. Sign. 6, pl1 (2013).
Hedau, S. et al. New germline mutations in breast most cancers susceptibility genes BRCA1, BRCA2 and p53 in breast most cancers sufferers in India. Breast most cancers Res. Deal with. 88, 177-186 (2004).
Chapman, J.R., Taylor, M.R. & Boulton, S.J. Play the ultimate recreation: Selecting the double-strand DNA restore pathway. Mol. Cell 47, 497-510 (2012).
Min, S.H. et al. Detrimental regulation of Fbw7 tumor suppression stability and performance by Pin1 prol1-isomerase. Mol. Cell 46, 771-783 (2012).
Lu, Ok.P., Finn, G., Lee, T.H. & Nicholson, L.Ok. Prolyl cis-trans isomerization as a molecular timer. Nat. Chem. Biol. three, 619-629 (2007).
Billing, D. et al. The BRCT domains of BRCA1 and BARD1 tumor suppressors differentially regulate homology-directed restore and safety of the blocked fork. Mol. Cell 72, 127-139 (2018).
Ding, X. et al. Artificial viability by insufficiency BRCA2 and PARP1 / ARTD1. Nat. Widespread. 7, 12425 (2016).
Berger, I., Fitzgerald, D.J. & Richmond, T.J. Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol. 22, 1583-1587 (2004).
Subramanyam, S., Ismail, M., Bhattacharya, I. & Spies, M. Tyrosine phosphorylation stimulates the exercise of human RAD51 recombinase by a modification of the nucleoprotein filament dynamics. Proc. Natl Acad. Sci. USA 113, E6045 to E6054 (2016).
Rueden, C. T. et al. ImageJ2: ImageJ for the following technology of scientific picture knowledge. BMC Bioinformatics 18, 529 (2017).