Abstract
The design of selective small molecules is often stymied by similar ligand binding pockets. Here, we report BSJ-03-123, a phthalimide-based degrader that exploits protein-interface determinants to achieve proteome-wide selectivity for the degradation of cyclin-dependent kinase 6 (CDK6). Pharmacologic CDK6 degradation targets a selective dependency of acute myeloid leukemia cells, and transcriptomics and phosphoproteomics profiling of acute degradation of CDK6 enabled dynamic mapping of its immediate role in coordinating signaling and transcription.
Keywords:
AML; CDK6; PROTAC; acute myeloid leukemia; molecular pharmacology; phosphoproteomics; selectivity; systems biology; targeted protein degradation; transcriptomics.
Copyright © 2018 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line, Tumor
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Cyclin-Dependent Kinase 4 / chemistry
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Cyclin-Dependent Kinase 4 / genetics
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Cyclin-Dependent Kinase 4 / metabolism
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Cyclin-Dependent Kinase 6 / chemistry
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Cyclin-Dependent Kinase 6 / genetics
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Cyclin-Dependent Kinase 6 / metabolism*
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Gene Expression / drug effects
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Gene Regulatory Networks / drug effects
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Humans
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Leukemia, Myeloid, Acute / metabolism
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Leukemia, Myeloid, Acute / pathology
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Phthalimides / chemistry
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Phthalimides / pharmacology
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Signal Transduction / drug effects
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Small Molecule Libraries / chemistry
Substances
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Phthalimides
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Small Molecule Libraries
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phthalimide
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CDK4 protein, human
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CDK6 protein, human
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Cyclin-Dependent Kinase 4
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Cyclin-Dependent Kinase 6