ik3-1/cables is a substrate for cyclin-dependent kinase 3 (cdk 3)

Tadanori Yamochi; Kentaro Semba; Keitaro Tsuji; Kiyohisa Mizumoto; Hiroko Sato; Yoshiharu Matsuura; Ikuo Nishimoto; Masaaki Matsuoka

doi:10.1046/j.0014-2956.2001.02555.x

ik3-1/cables is a substrate for cyclin-dependent kinase 3 (cdk 3)

Tadanori Yamochi, Kentaro Semba, Keitaro Tsuji, Kiyohisa Mizumoto, Hiroko Sato, Yoshiharu Matsuura, Ikuo Nishimoto, Masaaki Matsuoka^*

^*Corresponding author for this work

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

15 Citations (Scopus)

Abstract

p70^ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35^cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70^ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70^ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70^ik3-1 is upregulated. We therefore conclude that p70^ik3-1 is a substrate for cdk3-mediated phosphorylation.

Original language	English
Pages (from-to)	6076-6082
Number of pages	7
Journal	European Journal of Biochemistry
Volume	268
Issue number	23
DOIs	https://doi.org/10.1046/j.0014-2956.2001.02555.x
Publication status	Published - 2001
Externally published	Yes

Keywords

Phosphorylation
cdk3
ik3-1

ASJC Scopus subject areas

Biochemistry

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10.1046/j.0014-2956.2001.02555.x

Cite this

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title = "ik3-1/cables is a substrate for cyclin-dependent kinase 3 (cdk 3)",

abstract = "p70ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation.",

keywords = "Phosphorylation, cdk3, ik3-1",

author = "Tadanori Yamochi and Kentaro Semba and Keitaro Tsuji and Kiyohisa Mizumoto and Hiroko Sato and Yoshiharu Matsuura and Ikuo Nishimoto and Masaaki Matsuoka",

year = "2001",

doi = "10.1046/j.0014-2956.2001.02555.x",

language = "English",

volume = "268",

pages = "6076--6082",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell",

number = "23",

}

TY - JOUR

T1 - ik3-1/cables is a substrate for cyclin-dependent kinase 3 (cdk 3)

AU - Yamochi, Tadanori

AU - Semba, Kentaro

AU - Tsuji, Keitaro

AU - Mizumoto, Kiyohisa

AU - Sato, Hiroko

AU - Matsuura, Yoshiharu

AU - Nishimoto, Ikuo

AU - Matsuoka, Masaaki

PY - 2001

Y1 - 2001

N2 - p70ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation.

AB - p70ik3-1 (a 70-kDa protein) contains a cyclin box, and binds to p35cdk3 in vivo and in vitro [Matsuoka, M., Matsuura, Y., Semba, K. & Nishimoto, I. (2000) Biochem. Biophys. Res. Commun. 273, 442-447]. In spite of its structural similarity to cyclins, p70ik3-1 does not activate cyclin-dependent kinase 3 (cdk3)-mediated phosphorylation of pRb, histone H1, or the C-terminal domain of RNA polymerase II. Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation.

KW - Phosphorylation

KW - cdk3

KW - ik3-1

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U2 - 10.1046/j.0014-2956.2001.02555.x

DO - 10.1046/j.0014-2956.2001.02555.x

M3 - Article

C2 - 11733001

AN - SCOPUS:0035214117

SN - 0014-2956

VL - 268

SP - 6076

EP - 6082

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 23

ER -

ik3-1/cables is a substrate for cyclin-dependent kinase 3 (cdk 3)

Abstract

Keywords

ASJC Scopus subject areas

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