Abstract
Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.
| Original language | English (US) |
|---|---|
| Article number | 10 |
| Pages (from-to) | 157-164 |
| Number of pages | 8 |
| Journal | Methods in Enzymology |
| Volume | 399 |
| DOIs | |
| State | Published - 2005 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Analysis of ubiquitin chain-binding proteins by two-hybrid methods. / Apodaca, Jennifer; Ahn, Jungmi; Kim, Ikjin; Rao, Hai.
In: Methods in Enzymology, Vol. 399, 10, 2005, p. 157-164.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Analysis of ubiquitin chain-binding proteins by two-hybrid methods
AU - Apodaca, Jennifer
AU - Ahn, Jungmi
AU - Kim, Ikjin
AU - Rao, Hai
PY - 2005
Y1 - 2005
N2 - Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.
AB - Ubiquitin (Ub) regulates important cellular processes through covalent attachment to its substrates. Distinct fates are bestowed on multi-Ub chains linked through different lysine residues. Ub contains seven conserved lysines, all of which could be used for multi-Ub chain formation. K29 and K48 are the signals for proteasome-mediated proteolysis. Multi-Ub chains linked through K63 have nonproteolytic functions. Studies of Ub-binding factors are likely the key to understanding diverse functions of the Ub molecule. Yeast two-hybrid assay can be a powerful approach to dissect the interaction between Ub and its binding proteins and also the function of these Ub-chain binding proteins in vivo.
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UR - http://www.scopus.com/inward/citedby.url?scp=28844448199&partnerID=8YFLogxK
U2 - 10.1016/S0076-6879(05)99010-1
DO - 10.1016/S0076-6879(05)99010-1
M3 - Article
C2 - 16338354
AN - SCOPUS:28844448199
VL - 399
SP - 157
EP - 164
JO - Methods
JF - Methods
SN - 0076-6879
M1 - 10
ER -