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- 검색키워드
- 저자 : Clurman, Bruce E. (검색결과 2 건)
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NUP50 is necessary for the survival of primordial germ cells in mouse embryos
Park, Eunsook,Lee, Bobae,Clurman, Bruce E,Lee, Keesook Bioscientifica 2016 Reproduction Vol.151 No.1
<P>Nucleoporin 50 kDa (NUP50), a component of the nuclear pore complex, is highly expressed in male germ cells, but its role in germ cells is largely unknown. In this study, we analyzed the expression and function of NUP50 during the embryonic development of germ cells using NUP50-deficient mice. NUP50 was expressed in germ cells of both sexes at embryonic day 15.5 (E15.5), E13.5, and E12.5. In addition, NUP50 expression was also detected in primordial germ cells (PGCs) migrating into the genital ridges at E9.5. The gonads of <I>Nup50</I><I>−</I><I>/</I><I>−</I> embryos of both sexes contained few PGCs at both E11.5 and E12.5 and no developing germ cells at E15.5. The migratory PGCs in <I>Nup50</I><I>−</I><I>/</I><I>−</I> embryos at E9.5 showed increased apoptosis but a normal rate of proliferation, resulting in the progressive loss of germ cells at later stages. Taken together, these results suggest that NUP50 plays an essential role in the survival of PGCs during embryonic development.</P>
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Cand1 Promotes Assembly of New SCF Complexes through Dynamic Exchange of F Box Proteins
Pierce, Nathan W.,Lee, J.,Liu, X.,Sweredoski, Michael J.,Graham, Robert L.J.,Larimore, Elizabeth A.,Rome, M.,Zheng, N.,Clurman, Bruce E.,Hess, S.,Shan, S.o.,Deshaies, Raymond J. Cell Press ; MIT Press 2013 Cell Vol.153 No.1
The modular SCF (Skp1, cullin, and F box) ubiquitin ligases feature a large family of F box protein substrate receptors that enable recognition of diverse targets. However, how the repertoire of SCF complexes is sustained remains unclear. Real-time measurements of formation and disassembly indicate that SCF<SUP>Fbxw7</SUP> is extraordinarily stable, but, in the Nedd8-deconjugated state, the cullin-binding protein Cand1 augments its dissociation by one-million-fold. Binding and ubiquitylation assays show that Cand1 is a protein exchange factor that accelerates the rate at which Cul1-Rbx1 equilibrates with multiple F box protein-Skp1 modules. Depletion of Cand1 from cells impedes recruitment of new F box proteins to pre-existing Cul1 and profoundly alters the cellular landscape of SCF complexes. We suggest that catalyzed protein exchange may be a general feature of dynamic macromolecular machines and propose a hypothesis for how substrates, Nedd8, and Cand1 collaborate to regulate the cellular repertoire of SCF complexes.
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