期刊
JOURNAL OF CELLULAR BIOCHEMISTRY
卷 105, 期 6, 页码 1420-1429出版社
WILEY
DOI: 10.1002/jcb.21961
关键词
DEUBIQUITINATING ENZYME; PEST MOTIF; PROTEIN DEGRADATION; UBIQUITIN SPECIFIC PROTEASE
资金
- Korea Health 21 R & D Project, Ministry of Health, Welfare and Family Affairs [01-PJ10-PG6-01GN13-0002, A030003]
- Korea Health Promotion Institute [A010382] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ubiquitinaiton and deubiquitination of post-translational modification play counter roles in determining the fate of protein function in eukaryotic system for maintaining the cellular homeostasis. Even though novel family members of growth-regulating deubiquitinating enzymes (DUB-1 and DUB-2) have been identified, their target proteins and functions are poorly understood. Dub genes encoding DUB-1 and DUB-2 are immediate-early genes and are induced in response to cytokine stimuli rapidly and transiently. In order to explore the possible proteins regulated by DUB-1, we performed the matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis Followed by immunoprecipitation. We confirmed that DUB-1 interacts with dynein heavy chain, which is known to regulate the movement of organelles and microtubule binding ability. In addition, structural and immunoprecipitation analyses revealed that DUB-1 contains a putative PEST motif and is polyubiquitinated, indicating that DUB-1 is also regulated by the ubiquitin-proteasome pathway. J. Cell. Biochem. 105: 1420-1429, 2008. (C) 2008 Wiley-Liss. Inc.
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