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 - http://www.scopus.com/inward/record.url?scp=84874884921&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.422055
DO - 10.1074/jbc.M112.422055
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C2 - 23341463
AN - SCOPUS:84874884921
SN - 0021-9258
VL - 288
SP - 7294
EP - 7304
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 10
ER -