13 0

53BP1: A guardian for centrosomal integrity

Title
53BP1: A guardian for centrosomal integrity
Author
임형신
Keywords
53BP1; Stability; USP7; Mitosis; Centrosome; Review; DNA-DAMAGE RESPONSE; STRAND BREAK REPAIR; KINASE 1; HISTONE H2AX; CENP-F; HOMOLOGOUS RECOMBINATION; CHECKPOINT ACTIVATION; SPINDLE-CHECKPOINT; TUMOR-SUPPRESSOR; P53
Issue Date
2018-01
Publisher
FRONTIERS IN BIOSCIENCE INC
Citation
FRONTIERS IN BIOSCIENCE-LANDMARK, v. 23, Page. 1-12
Abstract
53BP1 is known as a mediator in DNA damage response and a regulator of DNA double-stranded breaks (DSBs) repair. 53BP1 was recently reported to be a centrosomal protein and a binding partner of mitotic polo-like kinase 1 (Plk1). The stability of 53BP1, in response to DSBs, is regulated by its phosphorylation, deubiquitination, and ubiquitination. During mitosis, 53BP1 is stabilized by phosphorylation at S380, a putative binding region with polo-box domain of Plk1, and deubiquitination by ubiquitin-specific protease 7 (USP7). In the absence of DSBs, 53BP1 is abundant in the nucleoplasm; DSB formation results in its rapid localization to the damaged chromatin. Mitotic 53BP1 is also localized at the centrosome and spindle pole. 53BP1 depletion induces mitotic defects such as disorientation of spindle poles attributed to extra centrosomes or mispositioning of centrosomes, leading to phenotypes similar to those in USP7-deficient cells. Here, we discuss how 53BP1 controls the centrosomal integrity through its interaction with USP7 and centromere protein F by regulation of its stability and its physiology in response to DNA damage.
URI
http://www.bioscience.org/2018/v23/af/4577/fulltext.htmhttp://repository.hanyang.ac.kr/handle/20.500.11754/105336
ISSN
1093-4715; 1093-9946
DOI
10.2741/4577
Appears in Collections:
COLLEGE OF PHARMACY[E](약학대학) > PHARMACY(약학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE