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Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/2468
Title: The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation
Authors: Lo, Wai Hong
Kan, Ho-Man
Chan, Ling-Nga
Xu, Wei-Guang
Wang, Ke-Peng
Wu, Zhenguo
Sheng, Morgan
Zhang, Mingjie
Keywords: Dynein
DNA damage
Proteins
Nuclear accumulation
Issue Date: Mar-2005
Citation: Journal of biological chemistry, v. 280, no. 9, Mar. 2005, p. 8172-8179
Abstract: The tumor suppressor protein p53 is known to undergo cytoplasmic dynein-dependent nuclear translocation in response to DNA damage. However, the molecular link between p53 and the minus end-directed microtubule motor dynein complex has not been described. We report here that the 8-kDa light chain (LC8) of dynein binds to p53-binding protein 1 (53BP1). The LC8-binding domain was mapped to a short peptide segment immediately N-terminal to the kinetochore localization region of 53BP1. The LC8-binding domain is completely separated from the p53-binding domain in 53BP1. Therefore, 53BP1 can potentially act as an adaptor to assemble p53 to the dynein complex. Unlike other known LC8-binding proteins, 53BP1 contains two distinct LC8-binding motifs that are arranged in tandem. We further showed that 53BP1 can directly associate with the dynein complex. Disruption of the interaction between LC8 and 53BP1 in vivo prevented DNA damage-induced nuclear accumulation of p53. These data illustrate that LC8 is able to function as a versatile acceptor to link a wide spectrum of molecular cargoes to the dynein motor.
Rights: We would like to give credit to American Society for Biochemistry and Molecular Biology for granting us permission to repost this article
URI: http://hdl.handle.net/1783.1/2468
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