Substrate Recognition and Ubiquitination of SCFSkp2/Cks1 Ubiquitin-Protein Isopeptide Ligase

p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evid...

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Published in	The Journal of biological chemistry Vol. 282; no. 21; pp. 15462 - 15470
Main Authors	Xu, Shuichan, Abbasian, Mahan, Patel, Palka, Jensen-Pergakes, Kristen, Lombardo, Christian R., Cathers, Brian E., Xie, Weilin, Mercurio, Frank, Pagano, Michele, Giegel, David, Cox, Sarah
Format	Journal Article
Language	English
Published	United States Elsevier Inc 25.05.2007 American Society for Biochemistry and Molecular Biology
Subjects	Animals Carrier Proteins - chemistry Carrier Proteins - metabolism CDC2-CDC28 Kinases Cell-Free System - chemistry Cell-Free System - metabolism Cyclin A - chemistry Cyclin A - metabolism Cyclin E - chemistry Cyclin E - metabolism Cyclin-Dependent Kinase 2 - chemistry Cyclin-Dependent Kinase 2 - metabolism Cyclin-Dependent Kinase Inhibitor p27 - chemistry Cyclin-Dependent Kinase Inhibitor p27 - metabolism Cyclin-Dependent Kinases - chemistry Cyclin-Dependent Kinases - metabolism G1 Phase - physiology Humans Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Phosphorylation Protein Processing, Post-Translational - physiology Recombinant Proteins - chemistry Recombinant Proteins - metabolism S Phase - physiology S-Phase Kinase-Associated Proteins - chemistry S-Phase Kinase-Associated Proteins - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism
Online Access	Get full text
ISSN	0021-9258 1083-351X
DOI	10.1074/jbc.M610758200

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Abstract	p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr187 on p27 are essential for the recognition of p27 by the SCFSkp2/Cks1 complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr187 provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2.
AbstractList	p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr187 on p27 are essential for the recognition of p27 by the SCFSkp2/Cks1 complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr187 provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2. p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr¹¸· on p27 are essential for the recognition of p27 by the SCFSkp²/Cks¹ complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr¹¸· provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2. p27, an important cell cycle regulator, blocks the G(1)/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr(187) on p27 are essential for the recognition of p27 by the SCF(Skp2/Cks1) complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr(187) provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2.p27, an important cell cycle regulator, blocks the G(1)/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr(187) on p27 are essential for the recognition of p27 by the SCF(Skp2/Cks1) complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr(187) provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2. p27, an important cell cycle regulator, blocks the G 1 /S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr 187 on p27 are essential for the recognition of p27 by the SCF Skp2/Cks1 complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr 187 provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2. p27, an important cell cycle regulator, blocks the G₁/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr¹⁸⁷ on p27 are essential for the recognition of p27 by the SCFSkp²/Cks¹ complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr¹⁸⁷ provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2. p27, an important cell cycle regulator, blocks the G(1)/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E). Ubiquitination and subsequent degradation play a critical role in regulating the levels of p27 during cell cycle progression. Here we provide evidence suggesting that both Cdk2/E and phosphorylation of Thr(187) on p27 are essential for the recognition of p27 by the SCF(Skp2/Cks1) complex, the ubiquitin-protein isopeptide ligase (E3). Cdk2/E provides a high affinity binding site, whereas the phosphorylated Thr(187) provides a low affinity binding site for the Skp2/Cks1 complex. Furthermore, binding of phosphorylated p27/Cdk2/E to the E3 complex showed positive cooperativity. Consistently, p27 is also ubiquitinated in a similarly cooperative manner. In the absence of p27, Cdk2/E and Cks1 increase Skp2 phosphorylation. This phosphorylation enhances Skp2 auto-ubiquitination, whereas p27 inhibits both phosphorylation and auto-ubiquitination of Skp2.
Author	Patel, Palka Xie, Weilin Abbasian, Mahan Mercurio, Frank Cox, Sarah Xu, Shuichan Lombardo, Christian R. Giegel, David Cathers, Brian E. Pagano, Michele Jensen-Pergakes, Kristen
Author_xml	– sequence: 1 givenname: Shuichan surname: Xu fullname: Xu, Shuichan email: sxu@celgene.com organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 2 givenname: Mahan surname: Abbasian fullname: Abbasian, Mahan organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 3 givenname: Palka surname: Patel fullname: Patel, Palka organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 4 givenname: Kristen surname: Jensen-Pergakes fullname: Jensen-Pergakes, Kristen organization: Department of Discovery Biology, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 5 givenname: Christian R. surname: Lombardo fullname: Lombardo, Christian R. organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 6 givenname: Brian E. surname: Cathers fullname: Cathers, Brian E. organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 7 givenname: Weilin surname: Xie fullname: Xie, Weilin organization: Department of Discovery Biology, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 8 givenname: Frank surname: Mercurio fullname: Mercurio, Frank organization: Department of Discovery Biology, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 9 givenname: Michele surname: Pagano fullname: Pagano, Michele organization: Department of Pathology and the Kaplan Comprehensive Cancer Center, New York University Medical Center, New York, New York 10016 – sequence: 10 givenname: David surname: Giegel fullname: Giegel, David organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121 – sequence: 11 givenname: Sarah surname: Cox fullname: Cox, Sarah organization: Department of Biochemistry and Biomarker Development, Signal Pharmaceuticals, LLC, San Diego, California 92121
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Snippet	p27, an important cell cycle regulator, blocks the G1/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E).... p27, an important cell cycle regulator, blocks the G₁/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E).... p27, an important cell cycle regulator, blocks the G 1 /S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E).... p27, an important cell cycle regulator, blocks the G(1)/S transition in cells by binding and inhibiting Cdk2/cyclin A and Cdk2/cyclin E complexes (Cdk2/E)....
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SubjectTerms	Animals Carrier Proteins - chemistry Carrier Proteins - metabolism CDC2-CDC28 Kinases Cell-Free System - chemistry Cell-Free System - metabolism Cyclin A - chemistry Cyclin A - metabolism Cyclin E - chemistry Cyclin E - metabolism Cyclin-Dependent Kinase 2 - chemistry Cyclin-Dependent Kinase 2 - metabolism Cyclin-Dependent Kinase Inhibitor p27 - chemistry Cyclin-Dependent Kinase Inhibitor p27 - metabolism Cyclin-Dependent Kinases - chemistry Cyclin-Dependent Kinases - metabolism G1 Phase - physiology Humans Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Phosphorylation Protein Processing, Post-Translational - physiology Recombinant Proteins - chemistry Recombinant Proteins - metabolism S Phase - physiology S-Phase Kinase-Associated Proteins - chemistry S-Phase Kinase-Associated Proteins - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism
Title	Substrate Recognition and Ubiquitination of SCFSkp2/Cks1 Ubiquitin-Protein Isopeptide Ligase
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