BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Zekun Guo; Wenwen Tang; Jian Yuan; Xinya Chen; Bo Wan; Xiuting Gu; Kuntian Luo; Yingli Wang; Long Yu

doi:10.1016/j.bbrc.2006.06.178

BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Zekun Guo, Wenwen Tang, Jian Yuan, Xinya Chen, Bo Wan, Xiuting Gu, Kuntian Luo, Yingli Wang, Long Yu

Pharmacology

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

14 Scopus citations

Abstract

Brain selective kinase 2 (BRSK2) has been identified as a member of AMPK related kinases. LKB1 can phosphorylate the Thr174 of BRSK2, increasing its activity >50-fold. In this study, we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. The association between these two proteins was confirmed by GST pull-down. Furthermore, our study indicated that the kinase activity of BRSK2 can be increased through phosphorylation by PKA.

Original language	English (US)
Pages (from-to)	867-871
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	347
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2006.06.178
State	Published - Sep 8 2006

Keywords

AMPK subfamily
BRSK2
PKA
Phosphorylation

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.06.178

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title = "BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260",

abstract = "Brain selective kinase 2 (BRSK2) has been identified as a member of AMPK related kinases. LKB1 can phosphorylate the Thr174 of BRSK2, increasing its activity >50-fold. In this study, we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. The association between these two proteins was confirmed by GST pull-down. Furthermore, our study indicated that the kinase activity of BRSK2 can be increased through phosphorylation by PKA.",

keywords = "AMPK subfamily, BRSK2, PKA, Phosphorylation",

author = "Zekun Guo and Wenwen Tang and Jian Yuan and Xinya Chen and Bo Wan and Xiuting Gu and Kuntian Luo and Yingli Wang and Long Yu",

note = "Funding Information: This work was supported by the National 973 program of China, 863 projects of China, and the National Natural Science foundation of China (30024001).",

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T1 - BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

AU - Guo, Zekun

AU - Tang, Wenwen

AU - Yuan, Jian

AU - Chen, Xinya

AU - Wan, Bo

AU - Gu, Xiuting

AU - Luo, Kuntian

AU - Wang, Yingli

AU - Yu, Long

N1 - Funding Information: This work was supported by the National 973 program of China, 863 projects of China, and the National Natural Science foundation of China (30024001).

PY - 2006/9/8

Y1 - 2006/9/8

N2 - Brain selective kinase 2 (BRSK2) has been identified as a member of AMPK related kinases. LKB1 can phosphorylate the Thr174 of BRSK2, increasing its activity >50-fold. In this study, we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. The association between these two proteins was confirmed by GST pull-down. Furthermore, our study indicated that the kinase activity of BRSK2 can be increased through phosphorylation by PKA.

AB - Brain selective kinase 2 (BRSK2) has been identified as a member of AMPK related kinases. LKB1 can phosphorylate the Thr174 of BRSK2, increasing its activity >50-fold. In this study, we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. The association between these two proteins was confirmed by GST pull-down. Furthermore, our study indicated that the kinase activity of BRSK2 can be increased through phosphorylation by PKA.

KW - AMPK subfamily

KW - BRSK2

KW - PKA

KW - Phosphorylation

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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ER -

BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Abstract

Keywords

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