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Critical lysine residues of Klf4 required for protein stabilization and degradation

Title
Critical lysine residues of Klf4 required for protein stabilization and degradation
Author
Ramakrishna Suresh
Keywords
Oncogene; Proteasomal degradation; Tumor suppressor; Ubiquitin; Ubiquitination; PLURIPOTENT STEM-CELLS; KRUPPEL-LIKE FACTOR-4; PROSTATE-CANCER; TRANSCRIPTION FACTOR; TUMOR-SUPPRESSOR; UBIQUITIN; PROTEASOME; SIGNALS; OCT4; MYC
Issue Date
2014-01
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
Citation
Biochemical and Biophysical Research Communications, Vol.443, No. 4, 24 January 2014, Pages 1206-1210
Abstract
The transcription factor, Kruppel-like factor 4 (Klf4) plays a crucial role in generating induced pluripotent stem cells (iPSCs). As the ubiquitination and degradation of the Klf4 protein have been suggested to play an important role in its function, the identification of specific lysine sites that are responsible for protein degradation is of prime interest to improve protein stability and function. However, the molecular mechanism regulating proteasomal degradation of the Klf4 is poorly understood. In this study, both the analysis of Klf4 ubiquitination sites using several Klf4 deletion fragments and bioinformatics predictions showed that the lysine sites which are signaling for Klf4 protein degradation lie in its N-terminal domain (aa 1-296). The results also showed that Lys32, 52,232, and 252 of Klf4 are responsible for the proteolysis of the Klf4 protein. These results suggest that Klf4 undergoes proteasomal degradation and that these lysine residues are critical for Klf4 ubiquitination. (C) 2013 Elsevier Inc. All rights reserved.
URI
https://www.sciencedirect.com/science/article/pii/S0006291X1302192Xhttp://hdl.handle.net/20.500.11754/47464
ISSN
0006-291X
DOI
10.1016/j.bbrc.2013.12.121
Appears in Collections:
GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > ETC
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