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Low‐density lipoprotein receptor‐related protein interacts with MafB, a regulator of hindbrain development
Author(s) -
Petersen Helle Heibroch,
Hilpert Jan,
Jacobsen Christian,
Lauwers Annick,
Roebroek Anton J.M.,
Willnow Thomas E.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.03.069
Subject(s) - microbiology and biotechnology , signal transducing adaptor protein , transcription factor , regulator , lrp1 , leucine zipper , atf3 , hindbrain , biology , ldl receptor , chemistry , signal transduction , lipoprotein , genetics , biochemistry , gene expression , gene , promoter , embryo , cholesterol
The intracellular domain (ICD) of the low‐density lipoprotein receptor‐related protein (LRP) functionally interacts with adaptor proteins both as an integral part of the receptor polypeptide and after proteolytic release. Identification of such adaptors has been difficult because the ICD is self‐activating in conventional transcription factor‐based yeast two‐hybrid screens. We adopted an alternative screen for the ICD that depends on the activation of the Ras‐signaling pathway and uncovered the transcription factor MafB as novel ICD interacting protein. MafB is a regulator of hindbrain segmentation and interacts with the ICD through a leucine zipper domain. The ICD co‐localizes with MafB to the nucleus and negatively regulates its transcriptional activity, suggesting a possible role for LRP in brain development.
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