Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135

Takuya Kojima; Yoshiaki Yoshikawa; Shinji Takada; Masahiro Sato; Takeshi Nakamura; Naoki Takahashi; Neal G. Copeland; Debra J. Gilbert; Nancy A. Jenkins; Nozomu Mori

doi:10.1006/bbrc.2001.5080

Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135

Takuya Kojima, Yoshiaki Yoshikawa, Shinji Takada, Masahiro Sato, Takeshi Nakamura, Naoki Takahashi, Neal G. Copeland, Debra J. Gilbert, Nancy A. Jenkins, Nozomu Mori

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

21 Scopus citations

Abstract

The Shc gene family is an emerging family, containing at least three members designated Shc/ShcA, Sck/Sli/ShcB, N-Shc/Rai/ShcC in mammals. In this study, we determined the genomic organization of the mouse Shc family. Coding regions of ShcA, B, and C each comprised 12 exons, spanned approximately 6, 20, and 65 kb, and located on chromosome 3, 10, and 13, respectively. Based on this genome analysis, we determined the full-length structure of mouse Sck/ShcB as a 68-kD protein. We found that the 68-kD full-length Sck/ShcB was more efficiently phosphorylated upon EGF treatment than the previously-analyzed CH2-deleted form. We also found that Sck specifically interacted with a 135-kD phosphoprotein (pp135) through its SH2 domain following membrane depolarization. The Sck-pp135 interaction was reduced by Src kinase inhibitors. These results suggest that Sck, but not N-Shc nor Shc, transmit signals in conjunction with pp135 following Src activation and/or calcium entry in the cell.

Original language	English (US)
Pages (from-to)	1039-1047
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	284
Issue number	4
DOIs	https://doi.org/10.1006/bbrc.2001.5080
State	Published - 2001

Keywords

Adapter
Genome
N-Shc
Phosphotyrosine
PTB
Sck
SH2
ShcB
ShcC
Signal transduction
Src

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1006/bbrc.2001.5080

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Kojima, T., Yoshikawa, Y., Takada, S., Sato, M., Nakamura, T., Takahashi, N., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., & Mori, N. (2001). Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135. Biochemical and Biophysical Research Communications, 284(4), 1039-1047. https://doi.org/10.1006/bbrc.2001.5080

Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135. / Kojima, Takuya; Yoshikawa, Yoshiaki; Takada, Shinji et al.
In: Biochemical and Biophysical Research Communications, Vol. 284, No. 4, 2001, p. 1039-1047.

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

Kojima, T, Yoshikawa, Y, Takada, S, Sato, M, Nakamura, T, Takahashi, N, Copeland, NG, Gilbert, DJ, Jenkins, NA & Mori, N 2001, 'Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135', Biochemical and Biophysical Research Communications, vol. 284, no. 4, pp. 1039-1047. https://doi.org/10.1006/bbrc.2001.5080

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title = "Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135",

abstract = "The Shc gene family is an emerging family, containing at least three members designated Shc/ShcA, Sck/Sli/ShcB, N-Shc/Rai/ShcC in mammals. In this study, we determined the genomic organization of the mouse Shc family. Coding regions of ShcA, B, and C each comprised 12 exons, spanned approximately 6, 20, and 65 kb, and located on chromosome 3, 10, and 13, respectively. Based on this genome analysis, we determined the full-length structure of mouse Sck/ShcB as a 68-kD protein. We found that the 68-kD full-length Sck/ShcB was more efficiently phosphorylated upon EGF treatment than the previously-analyzed CH2-deleted form. We also found that Sck specifically interacted with a 135-kD phosphoprotein (pp135) through its SH2 domain following membrane depolarization. The Sck-pp135 interaction was reduced by Src kinase inhibitors. These results suggest that Sck, but not N-Shc nor Shc, transmit signals in conjunction with pp135 following Src activation and/or calcium entry in the cell.",

keywords = "Adapter, Genome, N-Shc, Phosphotyrosine, PTB, Sck, SH2, ShcB, ShcC, Signal transduction, Src",

author = "Takuya Kojima and Yoshiaki Yoshikawa and Shinji Takada and Masahiro Sato and Takeshi Nakamura and Naoki Takahashi and Copeland, {Neal G.} and Gilbert, {Debra J.} and Jenkins, {Nancy A.} and Nozomu Mori",

note = "Funding Information: We thank Deborah B. Householder and Mary Barnstead for excellent technical assistance. The initial phase of this study was performed in the Laboratory of Inheritance and Variation that was supported by PRESTO, JST. This research was also supported, in part, by funds for Comprehensive Research on Aging and Health of the Ministry of Health and Welfare (to N.M.), by the Special Coordination Funds for Promoting Science and Technology (to N.M.), and by the National Cancer Institute, DHHS, under contract with ABL (to N.A.J.).",

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doi = "10.1006/bbrc.2001.5080",

language = "English (US)",

volume = "284",

pages = "1039--1047",

journal = "Biochemical and Biophysical Research Communications",

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T1 - Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB

T2 - Specific association of p68-Sck/ShcB with pp135

AU - Kojima, Takuya

AU - Yoshikawa, Yoshiaki

AU - Takada, Shinji

AU - Sato, Masahiro

AU - Nakamura, Takeshi

AU - Takahashi, Naoki

AU - Copeland, Neal G.

AU - Gilbert, Debra J.

AU - Jenkins, Nancy A.

AU - Mori, Nozomu

N1 - Funding Information: We thank Deborah B. Householder and Mary Barnstead for excellent technical assistance. The initial phase of this study was performed in the Laboratory of Inheritance and Variation that was supported by PRESTO, JST. This research was also supported, in part, by funds for Comprehensive Research on Aging and Health of the Ministry of Health and Welfare (to N.M.), by the Special Coordination Funds for Promoting Science and Technology (to N.M.), and by the National Cancer Institute, DHHS, under contract with ABL (to N.A.J.).

PY - 2001

Y1 - 2001

N2 - The Shc gene family is an emerging family, containing at least three members designated Shc/ShcA, Sck/Sli/ShcB, N-Shc/Rai/ShcC in mammals. In this study, we determined the genomic organization of the mouse Shc family. Coding regions of ShcA, B, and C each comprised 12 exons, spanned approximately 6, 20, and 65 kb, and located on chromosome 3, 10, and 13, respectively. Based on this genome analysis, we determined the full-length structure of mouse Sck/ShcB as a 68-kD protein. We found that the 68-kD full-length Sck/ShcB was more efficiently phosphorylated upon EGF treatment than the previously-analyzed CH2-deleted form. We also found that Sck specifically interacted with a 135-kD phosphoprotein (pp135) through its SH2 domain following membrane depolarization. The Sck-pp135 interaction was reduced by Src kinase inhibitors. These results suggest that Sck, but not N-Shc nor Shc, transmit signals in conjunction with pp135 following Src activation and/or calcium entry in the cell.

AB - The Shc gene family is an emerging family, containing at least three members designated Shc/ShcA, Sck/Sli/ShcB, N-Shc/Rai/ShcC in mammals. In this study, we determined the genomic organization of the mouse Shc family. Coding regions of ShcA, B, and C each comprised 12 exons, spanned approximately 6, 20, and 65 kb, and located on chromosome 3, 10, and 13, respectively. Based on this genome analysis, we determined the full-length structure of mouse Sck/ShcB as a 68-kD protein. We found that the 68-kD full-length Sck/ShcB was more efficiently phosphorylated upon EGF treatment than the previously-analyzed CH2-deleted form. We also found that Sck specifically interacted with a 135-kD phosphoprotein (pp135) through its SH2 domain following membrane depolarization. The Sck-pp135 interaction was reduced by Src kinase inhibitors. These results suggest that Sck, but not N-Shc nor Shc, transmit signals in conjunction with pp135 following Src activation and/or calcium entry in the cell.

KW - Adapter

KW - Genome

KW - N-Shc

KW - Phosphotyrosine

KW - PTB

KW - Sck

KW - SH2

KW - ShcB

KW - ShcC

KW - Signal transduction

KW - Src

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U2 - 10.1006/bbrc.2001.5080

DO - 10.1006/bbrc.2001.5080

M3 - Article

C2 - 11409899

AN - SCOPUS:0034809342

SN - 0006-291X

VL - 284

SP - 1039

EP - 1047

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Genomic organization of the Shc-related phosphotyrosine adapters and characterization of the full-length Sck/ShcB: Specific association of p68-Sck/ShcB with pp135

Abstract

Keywords

ASJC Scopus subject areas

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