Deubiquitinating enzyme USP36 contains the PEST motif and is polyubiquitinated.
The ubiquitin-mediated protein degradation pathway has been emphasized for the regulation of numerous cellular mechanisms and the significance of deubiquitination, mediated by deubiquitinating (DUB) enzymes, has been emerging as an essential regulatory step to control these cellular mechanisms. Previously, we demonstrated a human DUB enzyme, HeLa DUB-1, expressed in human ovarian cancer cells. Here, we report human USP36, which has the extension of the C-terminal region of HeLa DUB-1 and has conserved amino acid domains as previously shown in other DUBs. Human USP36, encoding a DUB enzyme, was isolated from ovarian cancer cells using RT-PCR and characterized. We identified DUB enzyme activity of USP36 by analyzing its capability to cleave the ubiquitin. Interestingly, structural and immunoprecipitation analyses revealed for the first time that USP36 contains the PEST motif and is polyubiquitinated.
Kim
Myung-Sun
MS
Graduate School of Life Science and Biotechnology, Pochon CHA University, CHA General Hospital, Seoul 135-081, Republic of Korea.
Kim
Yu-Kyung
YK
Kim
Yong-Soo
YS
Seong
Minu
M
Choi
Joong-Kook
JK
Baek
Kwang-Hyun
KH
D020816:Amino Acid Motifs; D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018076:DNA, Complementary / Q000235:genetics; D005091:Exons / Q000235:genetics; D005786:Gene Expression Regulation; D006801:Humans; D007438:Introns / Q000235:genetics; D051379:Mice; D011485:Protein Binding; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D025801:Ubiquitin / Q000378:metabolism*; D043222:Ubiquitin Thiolesterase
D018076:DNA, Complementary; D012333:RNA, Messenger; C501066:USP36 protein, human; D025801:Ubiquitin; D043222:Ubiquitin Thiolesterase; D003546:Cysteine Endopeptidases