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EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4

  1. Author:
    Kamata, T.
    Bong, Y. S.
    Mood, K.
    Park, M. J.
    Nishanian, T. G.
    Lee, H. S.

  2. Author Address

    [Kamata, Teddy; Bong, Yong-Sik; Mood, Kathleen; Nishanian, Tagvor G.; Lee, Hyun-Shik] NCI, Lab Cell & Dev Signaling, Frederick, MD 21702 USA. [Park, Mae Ja] Kyungpook Natl Univ, Dept Anat, Sch Med, Taegu 700422, South Korea. [Lee, Hyun-Shik] Kyungpook Natl Univ, Sch Life Sci, Coll Nat Sci, Taegu 702701, South Korea.;Lee, HS, NCI, Lab Cell & Dev Signaling, Frederick, MD 21702 USA.;tagvor@jertag.com leeh@knu.ac.kr
    1. Year: 2011
    2. Date: Mar
  2. Journal: Bmb Reports
    1. 44
    2. 3
    3. Pages: 199-204
  4. Type of Article: Article
  5. ISSN: 1976-6696
  1. Abstract:

    Ephrin signaling is involved in various morphogenetic events, such as axon guidance, hindbrain segmentation, and angiogenesis. We conducted a yeast two-hybrid screen using the intracellular domain (ICD) of EphrinB1 to gain biochemical insight into the function of the EphrinB1 ICD. We identified the transcriptional co-repressor xTLE1/Groucho as an EphrinB1 interacting protein. Whole-mount in situ hybridization of Xenopus embryos confirmed the co-localization of EphrinB1 and a Xenopus counterpart to TLE1, xTLE4, during various stages of development The EphrinB1/xTLE4 interaction was confirmed by co-immunoprecipitation experiments. Further characterization of the interaction revealed that the carboxy-terminal PDZ binding motif of EphrinB1 and the SP domain of xTLE4 are required for binding. Additionally, phosphorylation of EphrinB1 by a constitutively activated fibroblast growth factor receptor resulted in loss of the interaction, suggesting that the interaction is modulated by tyrosine phosphorylation of the EphrinB1 ICD. [BMB reports 2011; 44(3): 199-204]

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External Sources

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  2. DOI: 10.5483/BMBRep.2011.44.3.199
  3. View record in Web of Science®
  4. WOS: 000289051000009

Library Notes

  1. Fiscal Year: FY2010-2011
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