Recent progress with FKBP-derived destabilizing domains

Bernard W. Chu; Laura A. Banaszynski; Ling chun Chen; Thomas J. Wandless

doi:10.1016/j.bmcl.2008.09.043

Recent progress with FKBP-derived destabilizing domains

Bernard W. Chu, Laura A. Banaszynski, Ling chun Chen, Thomas J. Wandless

Research output: Contribution to journal › Article › peer-review

35 Scopus citations

Abstract

The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.

Original language	English (US)
Pages (from-to)	5941-5944
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	18
Issue number	22
DOIs	https://doi.org/10.1016/j.bmcl.2008.09.043
State	Published - Nov 15 2008

Keywords

Cell cycle
Cyclin
Destabilizing domain
Proteasome
Protein degradation
Shield-1

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2008.09.043

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title = "Recent progress with FKBP-derived destabilizing domains",

abstract = "The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.",

keywords = "Cell cycle, Cyclin, Destabilizing domain, Proteasome, Protein degradation, Shield-1",

author = "Chu, {Bernard W.} and Banaszynski, {Laura A.} and Chen, {Ling chun} and Wandless, {Thomas J.}",

note = "Funding Information: Financial support for these studies was provided by the NIH (GM073046). We thank Jim Ferrell and members of his lab for the Cyclin B1 gene and helpful advice. ",

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T1 - Recent progress with FKBP-derived destabilizing domains

AU - Chu, Bernard W.

AU - Banaszynski, Laura A.

AU - Chen, Ling chun

AU - Wandless, Thomas J.

N1 - Funding Information: Financial support for these studies was provided by the NIH (GM073046). We thank Jim Ferrell and members of his lab for the Cyclin B1 gene and helpful advice.

PY - 2008/11/15

Y1 - 2008/11/15

N2 - The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.

AB - The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.

KW - Cell cycle

KW - Cyclin

KW - Destabilizing domain

KW - Proteasome

KW - Protein degradation

KW - Shield-1

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JO - Bioorganic and Medicinal Chemistry Letters

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Recent progress with FKBP-derived destabilizing domains

Abstract

Keywords

ASJC Scopus subject areas

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