The cyclin-dependent kinase 11 interacts with NOT2

Jiaqi Shi; Mark A. Nelson

doi:10.1016/j.bbrc.2005.07.026

The cyclin-dependent kinase 11 interacts with NOT2

Jiaqi Shi, Mark A. Nelson

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

11 Scopus citations

Abstract

The caspase-processed cyclin-dependent kinase 11 (formerly known as PITSLRE) is implicated in apoptotic signaling. However, the mechanism of apoptotic signal transduction through CDK11^p46 is still unclear. We used a yeast two-hybrid screening strategy and identified NOT2 as an interacting partner of caspase-processed C-terminal kinase domain of CDK11 (CDK11 ^p46). We demonstrate that CDK11^p46 directly interacts with NOT2 in vitro and in human cells. The NOT domain in the C-terminal part of NOT2 is responsible for the association between CDK11^p46 and NOT2. Both NOT2 and CDK11^p46 predominantly co-localized in the nucleus. Furthermore, we show that overexpression of NOT2 reduces luciferase mRNA and induces apoptosis. However, NOT2 is not phosphorylated by CDK11^p46. These findings suggest that CDK11 may contribute to apoptosis by regulating the activity of NOT2 independent of its kinase activity.

Original language	English (US)
Pages (from-to)	1310-1316
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	334
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2005.07.026
State	Published - Sep 9 2005

Keywords

Apoptosis
CCR4-NOT complex
CDK11
Caspase
Cyclin-dependent kinase 11
NOT2
PITSLRE
Phosphorylation
RNA processing
Yeast two-hybrid

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2005.07.026

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title = "The cyclin-dependent kinase 11 interacts with NOT2",

abstract = "The caspase-processed cyclin-dependent kinase 11 (formerly known as PITSLRE) is implicated in apoptotic signaling. However, the mechanism of apoptotic signal transduction through CDK11p46 is still unclear. We used a yeast two-hybrid screening strategy and identified NOT2 as an interacting partner of caspase-processed C-terminal kinase domain of CDK11 (CDK11 p46). We demonstrate that CDK11p46 directly interacts with NOT2 in vitro and in human cells. The NOT domain in the C-terminal part of NOT2 is responsible for the association between CDK11p46 and NOT2. Both NOT2 and CDK11p46 predominantly co-localized in the nucleus. Furthermore, we show that overexpression of NOT2 reduces luciferase mRNA and induces apoptosis. However, NOT2 is not phosphorylated by CDK11p46. These findings suggest that CDK11 may contribute to apoptosis by regulating the activity of NOT2 independent of its kinase activity.",

keywords = "Apoptosis, CCR4-NOT complex, CDK11, Caspase, Cyclin-dependent kinase 11, NOT2, PITSLRE, Phosphorylation, RNA processing, Yeast two-hybrid",

author = "Jiaqi Shi and Nelson, {Mark A.}",

note = "Funding Information: We thank Dr. Vincent Kidd and Dr. Jill Lahti, St. Jude Children{\textquoteright}s Research Hospital, Memphis, Tennessee, for generously providing the P1C antibody. We thank Ms. Amy Ziemba, Dr. Richard Vaillancourt and Dr. Nancy Sachs for assistance in constructing the yeast two-hybrid baits and setting up the yeast two-hybrid screens. We thank Dr. Claire Payne for helping with the immunofluorescent staining. We also thank Dr. H.Th. Marc Timmers (University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands) for providing us the full-length NOT2 construct and NOT2 antibody. This research was supported by Grants CA70145 (MN), Center Grants ES066694 and CA 23074, and Cancer Biology Training Grant CA 09213.",

year = "2005",

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doi = "10.1016/j.bbrc.2005.07.026",

language = "English (US)",

volume = "334",

pages = "1310--1316",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

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TY - JOUR

T1 - The cyclin-dependent kinase 11 interacts with NOT2

AU - Shi, Jiaqi

AU - Nelson, Mark A.

N1 - Funding Information: We thank Dr. Vincent Kidd and Dr. Jill Lahti, St. Jude Children’s Research Hospital, Memphis, Tennessee, for generously providing the P1C antibody. We thank Ms. Amy Ziemba, Dr. Richard Vaillancourt and Dr. Nancy Sachs for assistance in constructing the yeast two-hybrid baits and setting up the yeast two-hybrid screens. We thank Dr. Claire Payne for helping with the immunofluorescent staining. We also thank Dr. H.Th. Marc Timmers (University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands) for providing us the full-length NOT2 construct and NOT2 antibody. This research was supported by Grants CA70145 (MN), Center Grants ES066694 and CA 23074, and Cancer Biology Training Grant CA 09213.

PY - 2005/9/9

Y1 - 2005/9/9

N2 - The caspase-processed cyclin-dependent kinase 11 (formerly known as PITSLRE) is implicated in apoptotic signaling. However, the mechanism of apoptotic signal transduction through CDK11p46 is still unclear. We used a yeast two-hybrid screening strategy and identified NOT2 as an interacting partner of caspase-processed C-terminal kinase domain of CDK11 (CDK11 p46). We demonstrate that CDK11p46 directly interacts with NOT2 in vitro and in human cells. The NOT domain in the C-terminal part of NOT2 is responsible for the association between CDK11p46 and NOT2. Both NOT2 and CDK11p46 predominantly co-localized in the nucleus. Furthermore, we show that overexpression of NOT2 reduces luciferase mRNA and induces apoptosis. However, NOT2 is not phosphorylated by CDK11p46. These findings suggest that CDK11 may contribute to apoptosis by regulating the activity of NOT2 independent of its kinase activity.

AB - The caspase-processed cyclin-dependent kinase 11 (formerly known as PITSLRE) is implicated in apoptotic signaling. However, the mechanism of apoptotic signal transduction through CDK11p46 is still unclear. We used a yeast two-hybrid screening strategy and identified NOT2 as an interacting partner of caspase-processed C-terminal kinase domain of CDK11 (CDK11 p46). We demonstrate that CDK11p46 directly interacts with NOT2 in vitro and in human cells. The NOT domain in the C-terminal part of NOT2 is responsible for the association between CDK11p46 and NOT2. Both NOT2 and CDK11p46 predominantly co-localized in the nucleus. Furthermore, we show that overexpression of NOT2 reduces luciferase mRNA and induces apoptosis. However, NOT2 is not phosphorylated by CDK11p46. These findings suggest that CDK11 may contribute to apoptosis by regulating the activity of NOT2 independent of its kinase activity.

KW - Apoptosis

KW - CCR4-NOT complex

KW - CDK11

KW - Caspase

KW - Cyclin-dependent kinase 11

KW - NOT2

KW - PITSLRE

KW - Phosphorylation

KW - RNA processing

KW - Yeast two-hybrid

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EP - 1316

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

The cyclin-dependent kinase 11 interacts with NOT2

Abstract

Keywords

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