Interactions of the Nijmegen Breakage Syndrome Protein with ATM and BRCA1

2000 ◽  
Vol 65 (0) ◽  
pp. 535-546 ◽  
Author(s):  
X. WU ◽  
G. RATHBUN ◽  
W.S. LANE ◽  
D.T. WEAVER ◽  
D.M. LIVINGSTON
Keyword(s):  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein

ATM phosphorylation of Nijmegen breakage syndrome protein is required in a DNA damage response

Nature ◽  
2000 ◽  
Vol 405 (6785) ◽  
pp. 477-482 ◽  
Author(s):  
Xiaohua Wu ◽  
Velvizhi Ranganathan ◽  
David S. Weisman ◽  
Walter F. Heine ◽  
David N. Ciccone ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Damage Response ◽  
Nijmegen Breakage Syndrome ◽  
Damage Response ◽  
Syndrome Protein

scholarly journals The Nijmegen Breakage Syndrome Protein Is Essential for Mre11 Phosphorylation upon DNA Damage

1999 ◽  
Vol 274 (28) ◽  
pp. 19513-19516 ◽  
Author(s):  
Zhiwan Dong ◽  
Qing Zhong ◽  
Phang-Lang Chen
Keyword(s):  
Dna Damage ◽  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein

Nijmegen Breakage Syndrome Protein (NBN) Causes Resistance to Methylating Anticancer Drugs Such as Temozolomide

2010 ◽  
Vol 78 (5) ◽  
pp. 943-951 ◽  
Author(s):  
Marcus Eich ◽  
Wynand P. Roos ◽  
Grigory L. Dianov ◽  
Martin Digweed ◽  
Bernd Kaina
Keyword(s):  
Anticancer Drugs ◽  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein

scholarly journals Functional deficiency of NBN, the Nijmegen breakage syndrome protein, in a p.R215W mutant breast cancer cell line

BMC Cancer ◽  
2014 ◽  
Vol 14 (1) ◽  
Author(s):  
Bianca Schröder-Heurich ◽  
Natalia Bogdanova ◽  
Britta Wieland ◽  
Xiaoxi Xie ◽  
Monika Noskowicz ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Line ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Breast Cancer Cell Line ◽  
Cancer Cell Line ◽  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein ◽  
Functional Deficiency

scholarly journals DNA repair: The Nijmegen breakage syndrome protein

1998 ◽  
Vol 8 (17) ◽  
pp. R622-R625 ◽  
Author(s):  
Carol Featherstone ◽  
Stephen P Jackson
Keyword(s):  
Dna Repair ◽  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein

scholarly journals SIRT1 Regulates the Function of the Nijmegen Breakage Syndrome Protein

2007 ◽  
Vol 27 (1) ◽  
pp. 149-162 ◽  
Author(s):  
Zhigang Yuan ◽  
Xiaohong Zhang ◽  
Nilanjan Sengupta ◽  
William S. Lane ◽  
Edward Seto
Keyword(s):  
Nijmegen Breakage Syndrome ◽  
Syndrome Protein

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

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