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  1. 紀要
  2. Tumor Research
  3. Vol.29

Multiple Proline-rich Regions of GAP-associated Phosphoprotein p62 Bind with Different Affinities to the Src Homology 3 Domains of Fyn and Src

https://doi.org/10.15114/tr.29.59
https://doi.org/10.15114/tr.29.59
2d86b2dc-7003-4725-9ebf-e7005e7192de
名前 / ファイル ライセンス アクション
n004140932959.pdf n004140932959.pdf (3.3 MB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2019-07-31
タイトル
タイトル Multiple Proline-rich Regions of GAP-associated Phosphoprotein p62 Bind with Different Affinities to the Src Homology 3 Domains of Fyn and Src
言語 en
言語
言語 eng
キーワード
言語 en
主題Scheme Other
主題 GAP-associated p62
キーワード
言語 en
主題Scheme Other
主題 Proline-rich
キーワード
言語 en
主題Scheme Other
主題 Protein-protein interaction
キーワード
言語 en
主題Scheme Other
主題 Protein tyrosine kinase
キーワード
言語 en
主題Scheme Other
主題 Src homology 3
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ departmental bulletin paper
ID登録
ID登録 10.15114/tr.29.59
ID登録タイプ JaLC
著者 Ishino, Masaho

× Ishino, Masaho

Ishino, Masaho

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Sasaki, Hiroko

× Sasaki, Hiroko

Sasaki, Hiroko

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Sasaki, Terukatsu

× Sasaki, Terukatsu

Sasaki, Terukatsu

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抄録
内容記述タイプ Abstract
内容記述 Several proteins of Jurkat cells were identified on SDS-PAGE gels by Coomassie Blue staining that bound specifically to affinity matrices made of five different Src homology 3 (SH3) domains fused to glutathione S-transferase (GST). Purification of the major specific band of approximately 70kDa with affinity beads of the SH3 domain of Fyn tyrosine kinase resulted in an identification of a GAP-associated p62-related protein as a ligand to the Fyn and Src SH3 domains. Indeed, from a lysate of a Rous sarcoma virus-transformed rat fibroblast line, Src co-precipitated with the 70kDa and also bound to a puta-tive SH3 binding sequence of p62. Bacterially expressed GST fusion proteins containing sequences encompassing each of the proline-rich putative SH3 binding sites of p62 bound to a subset of SH3 domains with different affinities. Phos-pholipase Cgannma 2-SH3 also revealed strong binding to the bacterially expressed p62 fusion proteins in vitro but did not show primary binding to the cellular 70kDa. The multiple SH3 binding sequences with different affinities to various SH3 mole-cules together with their phosphorylation on tyrosine residue(s) suggest a role of p62 as a foothold on which signal transduction proteins, including Src-family kinases, link together.
書誌情報 Tumor Research
en : Tumor Research

巻 29, p. 59-75, 発行日 1994
ISSN
収録物識別子タイプ ISSN
収録物識別子 0041-4093
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
出版者
出版者 Sapporo Medical University
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