Differential polyubiquitin recognition by tandem ubiquitin binding domains of Rabex-5
- Authors
- Shin, D[Shin, Donghyuk]; Lee, SY[Lee, Sei Young]; Han, S[Han, Seungsoo]; Ren, S[Ren, Shuo]; Kim, S[Kim, Soyoun]; Aikawa, Y[Aikawa, Yoshikatsu]; Lee, S[Lee, Sangho]
- Issue Date
- 13-Jul-2012
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Polyubiquitin; Rabex-5; Ubiquitin binding domain
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.423, no.4, pp.757 - 762
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 423
- Number
- 4
- Start Page
- 757
- End Page
- 762
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/64824
- DOI
- 10.1016/j.bbrc.2012.06.032
- ISSN
- 0006-291X
- Abstract
- Linkage-specific polyubiquitination regulates many cellular processes. The N-terminal fragment of Rabex-5 (Rabex-5(9-73)) contains tandem ubiquitin binding domains: A20_ZF and MIU. The A20_ZF-MIU of Rabex-5 is known to bind monoubiquitin but molecular details of polyubiquitin binding affinity and linkage selectivity by Rabex-5(9-73) remain elusive. Here we report that Rabex-5(9-73) binds linear, K63-and K48-linked tetraubiquitin (Ub(4)) chains with K-d of 0.1-1 mu M, determined by biolayer interferometry. Mutational analysis of qualitative and quantitative binding data reveals that MIU is more important than A20_ZF in linkage-specific polyubiquitin recognition. MIU prefers binding to linear and K63-linked Ub(4) with sub mu M affinities. However, A20_ZF recognizes the three linkage-specific Ub(4) with similar affinities with K-d of 3-4 mu M, unlike ZnF4 of A20. Taken together, our data suggest differential physiological roles of the two ubiquitin binding domains in Rabex-5. (C) 2012 Elsevier Inc. All rights reserved.
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Collections - Science > Department of Biological Science > 1. Journal Articles
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