Browsing Other ICR Research by author "Pearl, Laurence"
Now showing items 1-16 of 16
-
ATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT2 Domain with γH2AX.
Baldock, RA; Day, M; Wilkinson, OJ; Cloney, R; Jeggo, PA; et al. (CELL PRESS, 2015-12-15)53BP1 plays multiple roles in mammalian DNA damage repair, mediating pathway choice and facilitating DNA double-strand break repair in heterochromatin. Although it possesses a C-terminal BRCT2 domain, commonly involved in ... -
BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligands.
Day, M; Rappas, M; Ptasinska, K; Boos, D; Oliver, AW; et al. (ELIFE SCIENCES PUBLICATIONS LTD, 2018-10-08)TOPBP1 and its fission yeast homologueRad4, are critical players in a range of DNA replication, repair and damage signalling processes. They are composed of multiple BRCT domains, some of which bind phosphorylated motifs ... -
Differential Regulation of G1 CDK Complexes by the Hsp90-Cdc37 Chaperone System
Hallett, ST; Pastok, MW; Morgan, RML; Wittner, A; Blundell, KLIM; et al. (Elsevier BV, 2017-10-01) -
Efficient Single-Strand Break Repair Requires Binding to Both Poly(ADP-Ribose) and DNA by the Central BRCT Domain of XRCC1
Polo, LM; Xu, Y; Hornyak, P; Garces, F; Zeng, Z; et al. (Elsevier BV, 2019-01-01) -
HECTD3 Mediates an HSP90-Dependent Degradation Pathway for Protein Kinase Clients
Li, Z; Zhou, L; Prodromou, C; Savic, V; Pearl, LH (Elsevier BV, 2017-06-01) -
HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation.
Oberoi, J; Guiu, XA; Outwin, EA; Schellenberger, P; Roumeliotis, TI; et al. (NATURE PORTFOLIO, 2022-11-29)Activation of client protein kinases by the HSP90 molecular chaperone system is affected by phosphorylation at multiple sites on HSP90, the kinase-specific co-chaperone CDC37, and the kinase client itself. Removal of ... -
MDC1 Interacts with TOPBP1 to Maintain Chromosomal Stability during Mitosis.
Leimbacher, P-A; Jones, SE; Shorrocks, A-MK; de Marco Zompit, M; Day, M; et al. (CELL PRESS, 2019-05-02)In mitosis, cells inactivate DNA double-strand break (DSB) repair pathways to preserve genome stability. However, some early signaling events still occur, such as recruitment of the scaffold protein MDC1 to phosphorylated ... -
PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2B(Glu2).
Grundy, GJ; Polo, LM; Zeng, Z; Rulten, SL; Hoch, NC; et al. (Springer Science and Business Media LLC, 2016-08-17)PARP3 is a member of the ADP-ribosyl transferase superfamily that we show accelerates the repair of chromosomal DNA single-strand breaks in avian DT40 cells. Two-dimensional nuclear magnetic resonance experiments reveal ... -
Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1.
Day, M; Oliver, AW; Pearl, LH (ELSEVIER, 2021-10-19)The cellular response to DNA damage (DDR) that causes replication collapse and/or DNA double strand breaks, is characterised by a massive change in the post-translational modifications (PTM) of hundreds of proteins involved ... -
Phosphorylation-mediated interactions with TOPBP1 couple 53BP1 and 9-1-1 to control the G1 DNA damage checkpoint.
Bigot, N; Day, M; Baldock, RA; Watts, FZ; Oliver, AW; et al. (ELIFE SCIENCES PUBLICATIONS LTD, 2019-05-28)Coordination of the cellular response to DNA damage is organised by multi-domain 'scaffold' proteins, including 53BP1 and TOPBP1, which recognise post-translational modifications such as phosphorylation, methylation and ... -
Review: The HSP90 molecular chaperone—an enigmatic ATPase
Pearl, LH (Wiley, 2016-08-01)<jats:title>ABSTRACT</jats:title><jats:p>The HSP90 molecular chaperone is involved in the activation and cellular stabilization of a range of ‘client’ proteins, of which oncogenic protein kinases and nuclear steroid hormone ... -
RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex.
Martino, F; Pal, M; Muñoz-Hernández, H; Rodríguez, CF; Núñez-Ramírez, R; et al. (Springer Science and Business Media LLC, 2018-04-16)The R2TP/Prefoldin-like co-chaperone, in concert with HSP90, facilitates assembly and cellular stability of RNA polymerase II, and complexes of PI3-kinase-like kinases such as mTOR. However, the mechanism by which this ... -
Structural basis for the inactivation of cytosolic DNA sensing by the vaccinia virus.
Rivera-Calzada, A; Arribas-Bosacoma, R; Ruiz-Ramos, A; Escudero-Bravo, P; Boskovic, J; et al. (NATURE PORTFOLIO, 2022-11-18)Detection of cytosolic DNA is a central element of the innate immunity system against viral infection. The Ku heterodimer, a component of the NHEJ pathway of DNA repair in the nucleus, functions as DNA sensor that detects ... -
Structure of the human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp bound to a dsDNA-ssDNA junction.
Day, M; Oliver, AW; Pearl, LH (OXFORD UNIV PRESS, 2022-08-12)The RAD9-RAD1-HUS1 (9-1-1) clamp forms one half of the DNA damage checkpoint system that signals the presence of substantial regions of single-stranded DNA arising from replication fork collapse or resection of DNA double ... -
The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.
Grundy, GJ; Rulten, SL; Arribas-Bosacoma, R; Davidson, K; Kozik, Z; et al. (NATURE PUBLISHING GROUP, 2016-04-11)The Ku-binding motif (KBM) is a short peptide module first identified in APLF that we now show is also present in Werner syndrome protein (WRN) and in Modulator of retrovirus infection homologue (MRI). We also identify a ... -
Uncovering an allosteric mode of action for a selective inhibitor of human Bloom syndrome protein.
Chen, X; Ali, YI; Fisher, CE; Arribas-Bosacoma, R; Rajasekaran, MB; et al. (eLife Sciences Publications, Ltd, 2021-03-01)BLM (Bloom syndrome protein) is a RECQ-family helicase involved in the dissolution of complex DNA structures and repair intermediates. Synthetic lethality analysis implicates BLM as a promising target in a range of cancers ...