Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance

Ta Hsien Lin; Pai Chi Tsai; Hsin Tzu Liu; Yi Chen Chen; Lan Hsin Wang; Fu Kai Hsieh; Hsien Bin Huang

doi:10.1093/jb/mvi167

Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance

Ta Hsien Lin, Pai Chi Tsai, Hsin Tzu Liu, Yi Chen Chen, Lan Hsin Wang, Fu Kai Hsieh, Hsien Bin Huang^*

^*Corresponding author for this work

Department of Biochemistry

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

6 Scopus citations

Abstract

KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.

Original language	English
Pages (from-to)	697-700
Number of pages	4
Journal	Journal of Biochemistry
Volume	138
Issue number	6
DOIs	https://doi.org/10.1093/jb/mvi167
State	Published - Dec 2005

Keywords

Inhibitor-2
Protein phosphatase-1
Surface plasmon resonance

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10.1093/jb/mvi167

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@article{929d3a062c8b4f7aa67d84e4e8c74b05,

title = "Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance",

abstract = "KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.",

keywords = "Inhibitor-2, Protein phosphatase-1, Surface plasmon resonance",

author = "Lin, {Ta Hsien} and Tsai, {Pai Chi} and Liu, {Hsin Tzu} and Chen, {Yi Chen} and Wang, {Lan Hsin} and Hsieh, {Fu Kai} and Huang, {Hsien Bin}",

note = "Funding Information: This work was supported by Grants from the National Science Council of the Republic of China (NSC 92-2320-B-194-005 and NSC 92-2311-B-010-003), the Taipei Veterans General Hospital Taiwan, Republic of China.",

year = "2005",

month = dec,

doi = "10.1093/jb/mvi167",

language = "English",

volume = "138",

pages = "697--700",

journal = "Journal of Biochemistry",

issn = "0021-924X",

publisher = "Oxford University Press",

number = "6",

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TY - JOUR

T1 - Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance

AU - Lin, Ta Hsien

AU - Tsai, Pai Chi

AU - Liu, Hsin Tzu

AU - Chen, Yi Chen

AU - Wang, Lan Hsin

AU - Hsieh, Fu Kai

AU - Huang, Hsien Bin

N1 - Funding Information: This work was supported by Grants from the National Science Council of the Republic of China (NSC 92-2320-B-194-005 and NSC 92-2311-B-010-003), the Taipei Veterans General Hospital Taiwan, Republic of China.

PY - 2005/12

Y1 - 2005/12

N2 - KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.

AB - KLHY is a short amino-acid sequence of inhibitor-2. This sequence is highly conserved with the protein phosphatase 1 (PP1)-binding consensus motif, RVXF. The role of this segment in binding with PP1 is ambiguous. By using surface plasmon resonance we have characterized its binding ability to PP1. Either site-directed mutagenesis or deletion of KLHY did not significantly affect the dissociation constant between PP1 and inhibitor-2. In comparison with DARPP-32, the deletion of KKIQF, a PP1-binding motif of DARPP-32, resulted in a remarkable reduction in its affinity with PP1. Our results suggested that, compared with the common RVXF motif, the KLHY sequence in intact inhibitor-2 binds weakly to PP1.

KW - Inhibitor-2

KW - Protein phosphatase-1

KW - Surface plasmon resonance

UR - http://www.scopus.com/inward/record.url?scp=32944456219&partnerID=8YFLogxK

U2 - 10.1093/jb/mvi167

DO - 10.1093/jb/mvi167

M3 - Article

C2 - 16428298

AN - SCOPUS:32944456219

SN - 0021-924X

VL - 138

SP - 697

EP - 700

JO - Journal of Biochemistry

JF - Journal of Biochemistry

IS - 6

ER -

Characterization of the protein phosphatase 1-binding motifs of inhibitor-2 and DARPP-32 by surface plasmon resonance

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