Journal
BIOCHEMICAL JOURNAL
Volume 399, Issue -, Pages 397-404Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20060441
Keywords
dimerization; immunoprecipitation; oligomerization; presenilin; ubiquilin; yeast two-hydrid assay
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Funding
- NIA NIH HHS [R01 AG016839, AG016839] Funding Source: Medline
- NIGMS NIH HHS [GM066287, T32 GM008181, T32 GM08181, R01 GM066287] Funding Source: Medline
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Ubiquilin proteins have been shown to interact with a wide variety of other cellular proteins, often regulating the stability and degradation of the interacting protein. Ubiquilin contains a UBL (ubiquitin-like) domain at the N-terminus and a UBA (ubiquitin-associated) domain at the C-terminus, separated by a central region containing Stil-like repeats. Little is known about regulation of the interaction of ubiquilin with other proteins. In the present study, we show that ubiquilin is capable of forming dimers, and that dimerization requires the central region of ubiquilin, but not its UBL or the UBA domains. Furthermore, we provide evidence suggesting that monomeric ubiquilin is likely to be the active form that is involved in binding presenilin proteins. Our results provide new insight into the regulatory mechanism underlying the interaction of ubiquilin with presemlins.
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