TY - JOUR
T1 - Nuclear deubiquitination in the spotlight
T2 - the multifaceted nature of USP7 biology in disease
AU - Rawat, Radhika
AU - Starczynowski, Daniel T.
AU - Ntziachristos, Panagiotis
N1 - Funding Information:
The authors have been supported by an NIHT32 CA009560 Carcinogenesis Training Grant (to R. Rawat), and by NCI (R00CA188293), the National Science Foundation, the American Society of Hematology, the Leukemia Research Foundation, the St. Baldrick's Foundation, the H Foundation, the Gabrielle's Angel Foundation, The Hartwell Foundation, the Elsa U. Pardee Foundation, a Gilead Research Scholarship and the Zell Foundation (to P. Ntziachristos).
Funding Information:
The authors have been supported by an NIH T32 CA009560 Carcinogenesis Training Grant (to R. Rawat), and by NCI ( R00CA188293 ), the National Science Foundation , the American Society of Hematology , the Leukemia Research Foundation , the St. Baldrick’s Foundation , the H Foundation , the Gabrielle’s Angel Foundation , The Hartwell Foundation , the Elsa U. Pardee Foundation , a Gilead Research Scholarship and the Zell Foundation (to P. Ntziachristos).
PY - 2019/6
Y1 - 2019/6
N2 - Ubiquitination is a versatile and tightly regulated post-translational protein modification with many distinct outcomes affecting protein stability, localization, interactions, and activity. Ubiquitin chain linkages anchored on substrates can be further modified by additional post-translational modifications, including phosphorylation and SUMOylation. Deubiquitinases (DUBs) reverse these ubiquitin marks with matched levels of precision. Over hundred known DUBs regulate a wide variety of cellular events. In this review, we focus on ubiquitin-specific protease 7 (USP7, also known as herpesvirus-associated ubiquitin-specific protease, or HAUSP) as one of the best studied, disease-associated DUBs. By highlighting the functions of USP7, particularly in the nucleus, and the emergence of the newest generation of USP7 inhibitors, we illustrate the importance of individual DUBs in the nucleus, and the therapeutic prospects of DUB targeting in human disease.
AB - Ubiquitination is a versatile and tightly regulated post-translational protein modification with many distinct outcomes affecting protein stability, localization, interactions, and activity. Ubiquitin chain linkages anchored on substrates can be further modified by additional post-translational modifications, including phosphorylation and SUMOylation. Deubiquitinases (DUBs) reverse these ubiquitin marks with matched levels of precision. Over hundred known DUBs regulate a wide variety of cellular events. In this review, we focus on ubiquitin-specific protease 7 (USP7, also known as herpesvirus-associated ubiquitin-specific protease, or HAUSP) as one of the best studied, disease-associated DUBs. By highlighting the functions of USP7, particularly in the nucleus, and the emergence of the newest generation of USP7 inhibitors, we illustrate the importance of individual DUBs in the nucleus, and the therapeutic prospects of DUB targeting in human disease.
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U2 - 10.1016/j.ceb.2019.02.008
DO - 10.1016/j.ceb.2019.02.008
M3 - Review article
C2 - 30897496
AN - SCOPUS:85063013527
VL - 58
SP - 85
EP - 94
JO - Current Opinion in Cell Biology
JF - Current Opinion in Cell Biology
SN - 0955-0674
ER -