Identification of LRP1B-interacting proteins and inhibition of protein kinase Calpha-phosphorylation of LRP1B by association with PICK1.

Abstract:

: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 PKCalpha 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 PKCalpha phosphorylation of LRP1B.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Shiroshima T,Oka C,Kawaichi M

doi

10.1016/j.febslet.2008.11.045

subject

Has Abstract

pub_date

2009-01-05 00:00:00

pages

43-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(08)00961-7

journal_volume

583

pub_type

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