Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins

Ksenya Cohen-Katsenelson; Tanya Wasserman; Ilona Darlyuk-Saadon; Alona Rabner; Fabian Glaser; Ami Aronheim

doi:10.1074/jbc.M112.422055

Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins

Ksenya Cohen-Katsenelson
, Tanya Wasserman
, Ilona Darlyuk-Saadon
, Alona Rabner
, Fabian Glaser
, Ami Aronheim

Technion - Israel Institute of Technology

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

Abstract

Background: WDR62 is a JNK scaffold protein. Results: We identified at the WDR62 C terminus a loop-helix domain that is responsible for its homodimerization and association with another JNK scaffold protein, MAPKBP1. WDR62 dimerization is required for JNK and MKK7β1 recruitment. Conclusion: WDR62 dimerization is required for its scaffolding function. Significance: Scaffold protein association offers another layer of complexity for the fine tuning of signaling pathways.

Original language	English
Pages (from-to)	7294-7304
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M112.422055
State	Published - 8 Mar 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M112.422055

Cite this

@article{7308c2bb2f5f4dcb863aca6eb42907a6,

title = "Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins",

abstract = "Background: WDR62 is a JNK scaffold protein. Results: We identified at the WDR62 C terminus a loop-helix domain that is responsible for its homodimerization and association with another JNK scaffold protein, MAPKBP1. WDR62 dimerization is required for JNK and MKK7β1 recruitment. Conclusion: WDR62 dimerization is required for its scaffolding function. Significance: Scaffold protein association offers another layer of complexity for the fine tuning of signaling pathways.",

author = "Ksenya Cohen-Katsenelson and Tanya Wasserman and Ilona Darlyuk-Saadon and Alona Rabner and Fabian Glaser and Ami Aronheim",

year = "2013",

month = mar,

day = "8",

doi = "10.1074/jbc.M112.422055",

language = "English",

volume = "288",

pages = "7294--7304",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "10",

}

TY - JOUR

T1 - Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins

AU - Cohen-Katsenelson, Ksenya

AU - Wasserman, Tanya

AU - Darlyuk-Saadon, Ilona

AU - Rabner, Alona

AU - Glaser, Fabian

AU - Aronheim, Ami

PY - 2013/3/8

Y1 - 2013/3/8

N2 - Background: WDR62 is a JNK scaffold protein. Results: We identified at the WDR62 C terminus a loop-helix domain that is responsible for its homodimerization and association with another JNK scaffold protein, MAPKBP1. WDR62 dimerization is required for JNK and MKK7β1 recruitment. Conclusion: WDR62 dimerization is required for its scaffolding function. Significance: Scaffold protein association offers another layer of complexity for the fine tuning of signaling pathways.

AB - Background: WDR62 is a JNK scaffold protein. Results: We identified at the WDR62 C terminus a loop-helix domain that is responsible for its homodimerization and association with another JNK scaffold protein, MAPKBP1. WDR62 dimerization is required for JNK and MKK7β1 recruitment. Conclusion: WDR62 dimerization is required for its scaffolding function. Significance: Scaffold protein association offers another layer of complexity for the fine tuning of signaling pathways.

UR - https://www.scopus.com/pages/publications/84874884921

U2 - 10.1074/jbc.M112.422055

DO - 10.1074/jbc.M112.422055

M3 - Article

C2 - 23341463

SN - 0021-9258

VL - 288

SP - 7294

EP - 7304

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 10

ER -

Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this