Analysis of ubiquitin chain-binding proteins by two-hybrid methods

Jennifer Apodaca; Jungmi Ahn; Ikjin Kim; Hai Rao

doi:10.1016/S0076-6879(05)99010-1

Analysis of ubiquitin chain-binding proteins by two-hybrid methods

Jennifer Apodaca, Jungmi Ahn, Ikjin Kim, Hai Rao

Molecular Medicine

Research output: Contribution to journal › Review article › peer-review

1 Scopus citations

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	https://doi.org/10.1016/S0076-6879(05)99010-1
State	Published - 2005

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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title = "Analysis of ubiquitin chain-binding proteins by two-hybrid methods",

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.",

author = "Jennifer Apodaca and Jungmi Ahn and Ikjin Kim and Hai Rao",

note = "Funding Information: We are grateful to S. Fields, T. Ito, and the Yeast Resource Center for strains and plasmids. This work was supported by grants to H. R. from San Antonio Cancer Institute, San Antonio Area Foundation, UT Health Science Center HHMI Research Resources Program, and UT Health Science Center Institutional Research Grant.",

year = "2005",

doi = "10.1016/S0076-6879(05)99010-1",

language = "English (US)",

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pages = "157--164",

journal = "ImmunoMethods",

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T1 - Analysis of ubiquitin chain-binding proteins by two-hybrid methods

AU - Apodaca, Jennifer

AU - Ahn, Jungmi

AU - Kim, Ikjin

AU - Rao, Hai

N1 - Funding Information: We are grateful to S. Fields, T. Ito, and the Yeast Resource Center for strains and plasmids. This work was supported by grants to H. R. from San Antonio Cancer Institute, San Antonio Area Foundation, UT Health Science Center HHMI Research Resources Program, and UT Health Science Center Institutional Research Grant.

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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Analysis of ubiquitin chain-binding proteins by two-hybrid methods

Abstract

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