Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains

Tanaka, Hiroaki; Akagi, Ken-ichi; Oneyama, Chitose; Tanaka, Masakazu; Sasaki, Yuichi; Kanou, Takashi; Lee, Young-Ho; Yokogawa, Daisuke; Dobenecker, Marc-Werner; Nakagawa, Atushi; Okada, Masato; Ikegami, Takahisa

doi:https://doi.org/10.1074/jbc.M112.439075

Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains

Tanaka, Hiroaki; Akagi, Ken-ichi; Oneyama, Chitose et al.

Journal of Biological Chemistry, 2013, 288(21), 15240-15254

Number of Access:1,609（2025-09-29 10:02 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73661

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Title	Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains
Creator	CreatorName Tanaka, Hiroaki
	CreatorName Akagi, Ken-ichi
	NRID 1000090373208 1000090373208 CreatorName Oneyama, Chitose
	NRID 1000000227175 1000000227175 CreatorName Tanaka, Masakazu
	CreatorName Sasaki, Yuichi
	NRID 1000070528455 1000070528455 researchmap permalink tkanou tkanou Scopus Author ID 55241221000 55241221000 CreatorName Kanou, Takashi
	NRID 1000070589431 1000070589431 CreatorName Lee, Young-Ho
	NRID 1000090624239 1000090624239 CreatorName Yokogawa, Daisuke
	CreatorName Dobenecker, Marc-Werner
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 CreatorName Nakagawa, Atushi
	NRID 1000010177058 1000010177058 researchmap permalink read0185193 read0185193 Scopus Author ID 35300403700 35300403700 CreatorName Okada, Masato
	NRID 1000020283939 1000020283939 CreatorName Ikegami, Takahisa
Description	This research was originally published in Journal of Biological Chemistry. Hiroaki Tanaka, Ken-ichi Akagi, Chitose Oneyama, Masakazu Tanaka, Yuichi Sasaki, Takashi Kanou, Young-Ho Lee, Daisuke Yokogawa, Marc-Werner Dobenecker, Atsushi Nakagawa, Masato Okada and Takahisa Ikegami. Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains. Journal of Biological Chemistry. 2013; 288, 15240-15254. © the American Society for Biochemistry and Molecular Biology.
Abstract	Proteins with Src homology 2 (SH2) domains play major roles in tyrosine kinase signaling. Structures of many SH2 domains have been studied, and the regions involved in their interactions with ligands have been elucidated. However, these analyses have been performed using short peptides consisting of phosphotyrosine followed by a few amino acids, which are described as the canonical recognition sites. Here, we report the solution structure of the SH2 domain of C-terminal Src kinase (Csk) in complex with a longer phosphopeptide from the Csk-binding protein (Cbp). This structure, together with biochemical experiments, revealed the existence of a novel binding region in addition to the canonical phosphotyrosine 314-binding site of Cbp. Mutational analysis of this second region in cells showed that both canonical and novel binding sites are required for tumor suppression through the Cbp-Csk interaction. Furthermore, the data indicate an allosteric connection between Cbp binding and Csk activation that arises from residues in the βB/βCloop of the SH2 domain.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	288(21)
Page	15240-15254
Date of Issued	2013-05
Language	English
Handle URL	https://hdl.handle.net/11094/73661
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M112.439075
Relation.isIdenticalTo	PMID 23548896
Access Rights	open access
CopyRight	© the American Society for Biochemistry and Molecular Biology.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2013, 288(21), p. 15240-15254
DC.title	Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains
DC.creator	Tanaka, Hiroaki
	Akagi, Ken-ichi
	Oneyama, Chitose
	Tanaka, Masakazu
	Sasaki, Yuichi
	Kanou, Takashi
	Lee, Young-Ho
	Yokogawa, Daisuke
	Dobenecker, Marc-Werner
	Nakagawa, Atushi
	Okada, Masato
	Ikegami, Takahisa
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2013-05
DC.identifier	https://doi.org/10.1074/jbc.M112.439075
DC.description	This research was originally published in Journal of Biological Chemistry. Hiroaki Tanaka, Ken-ichi Akagi, Chitose Oneyama, Masakazu Tanaka, Yuichi Sasaki, Takashi Kanou, Young-Ho Lee, Daisuke Yokogawa, Marc-Werner Dobenecker, Atsushi Nakagawa, Masato Okada and Takahisa Ikegami. Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains. Journal of Biological Chemistry. 2013; 288, 15240-15254. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	Proteins with Src homology 2 (SH2) domains play major roles in tyrosine kinase signaling. Structures of many SH2 domains have been studied, and the regions involved in their interactions with ligands have been elucidated. However, these analyses have been performed using short peptides consisting of phosphotyrosine followed by a few amino acids, which are described as the canonical recognition sites. Here, we report the solution structure of the SH2 domain of C-terminal Src kinase (Csk) in complex with a longer phosphopeptide from the Csk-binding protein (Cbp). This structure, together with biochemical experiments, revealed the existence of a novel binding region in addition to the canonical phosphotyrosine 314-binding site of Cbp. Mutational analysis of this second region in cells showed that both canonical and novel binding sites are required for tumor suppression through the Cbp-Csk interaction. Furthermore, the data indicate an allosteric connection between Cbp binding and Csk activation that arises from residues in the βB/βCloop of the SH2 domain.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73661
citation_title	Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains
citation_author	Tanaka, Hiroaki
	Akagi, Ken-ichi
	Oneyama, Chitose
	Tanaka, Masakazu
	Sasaki, Yuichi
	Kanou, Takashi
	Lee, Young-Ho
	Yokogawa, Daisuke
	Dobenecker, Marc-Werner
	Nakagawa, Atushi
	Okada, Masato
	Ikegami, Takahisa
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2013-05
citation_journal_title	Journal of Biological Chemistry
citation_volume	288
citation_issue	21
citation_firstpage	15240
citation_lastpage	15254
citation_doi	https://doi.org/10.1074/jbc.M112.439075
citation_pmid	23548896
citation_public_url	https://hdl.handle.net/11094/73661

Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains

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