Identification and characterization of modular domains that bind ubiquitin

Michael French; Kurt Swanson; Susan C. Shih; Ishwar Radhakrishnan; Linda Hicke

doi:10.1016/S0076-6879(05)99009-5

Identification and characterization of modular domains that bind ubiquitin

Michael French^*, Kurt Swanson, Susan C. Shih, Ishwar Radhakrishnan, Linda Hicke

^*Corresponding author for this work

Robert H. Lurie Comprehensive Cancer Center

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

13 Scopus citations

Abstract

To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.

Original language	English (US)
Article number	9
Pages (from-to)	135-157
Number of pages	23
Journal	Methods in enzymology
Volume	399
DOIs	https://doi.org/10.1016/S0076-6879(05)99009-5
State	Published - 2005

Funding

This work was supported by grants from the National Institutes of Health to I. R. and L. H. K. A. S. was supported by an NIH Molecular Biophysics training grant. I. R. is a Scholar of the Leukemia and Lymphoma Society. Support from the Robert H. Lurie Comprehensive Cancer Center for structural biology research at Northwestern University is gratefully acknowledged.

ASJC Scopus subject areas

Molecular Biology
Biochemistry

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10.1016/S0076-6879(05)99009-5

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title = "Identification and characterization of modular domains that bind ubiquitin",

abstract = "To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.",

author = "Michael French and Kurt Swanson and Shih, {Susan C.} and Ishwar Radhakrishnan and Linda Hicke",

note = "Funding Information: This work was supported by grants from the National Institutes of Health to I. R. and L. H. K. A. S. was supported by an NIH Molecular Biophysics training grant. I. R. is a Scholar of the Leukemia and Lymphoma Society. Support from the Robert H. Lurie Comprehensive Cancer Center for structural biology research at Northwestern University is gratefully acknowledged.",

year = "2005",

doi = "10.1016/S0076-6879(05)99009-5",

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journal = "Methods in enzymology",

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T1 - Identification and characterization of modular domains that bind ubiquitin

AU - French, Michael

AU - Swanson, Kurt

AU - Shih, Susan C.

AU - Radhakrishnan, Ishwar

AU - Hicke, Linda

N1 - Funding Information: This work was supported by grants from the National Institutes of Health to I. R. and L. H. K. A. S. was supported by an NIH Molecular Biophysics training grant. I. R. is a Scholar of the Leukemia and Lymphoma Society. Support from the Robert H. Lurie Comprehensive Cancer Center for structural biology research at Northwestern University is gratefully acknowledged.

PY - 2005

Y1 - 2005

N2 - To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.

AB - To receive and transmit the information carried by ubiquitin signals, cells have evolved an array of modular ubiquitin-binding domains. These domains bind directly and noncovalently to monoubiquitin and polyubiquitin chains and are found within proteins that function in diverse biological processes. Ubiquitin-binding domains characterized thus far are generally small and structurally diverse, yet they all interact with the same hydrophobic patch on the surface of ubiquitin. The rapid identification and characterization of ubiquitin-binding domains has been accomplished through the extensive use of bioinformatics, biochemistry, molecular biology, and biophysics. Here, we discuss the strategies and tools that have been most successful in the identification and characterization of ubiquitin-binding domains.

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DO - 10.1016/S0076-6879(05)99009-5

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AN - SCOPUS:28844453261

SN - 0076-6879

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SP - 135

EP - 157

JO - Methods in enzymology

JF - Methods in enzymology

M1 - 9

ER -

Identification and characterization of modular domains that bind ubiquitin

Abstract

Funding

ASJC Scopus subject areas

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