Journal
FEBS LETTERS
Volume 583, Issue 1, Pages 43-48Publisher
WILEY
DOI: 10.1016/j.febslet.2008.11.045
Keywords
LDL receptor family; LRP1B; LRP1; PICK1; JIP; PDZ domain; Protein kinase C
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Recent studies show LDL receptor-related protein 1B, LRP1B as a transducer of extracellular signals. Here, we identify six interacting partners of the LRP1B cytoplasmic region by yeast two-hybrid screen and confirmed their in vivo binding by immunoprecipitation. One of the partners, PICK1 recognizes the C-terminus of LRP1B and LRP1. The cytoplasmic domains of LRP1B are phosphorylated by PKC alpha about 100 times more efficiently than LRP1. Binding of PICK1 inhibits phosphorylation of LRP1B, but does not affect LRP1 phosphorylation. This study presents the possibility that LRP1B participates in signal transduction which PICK1 may regulate by inhibiting PKC alpha phosphorylation of LRP1B.
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