Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Trends Cardiovasc. Med. May (2002); 12(4):160-5 Phosphorylation of LRP1: regulation of transport and signal transduction. van der Geer P Department of Chemistry and Biochemistry, University of California San Diego, La Jolla 92093-0601, USA. geer@ucsd.edu Abstract: Low-density lipoprotein receptor-related protein 1 (LRP1) is a member of the low-density lipoprotein receptor family. Members of this family were once thought to be involved exclusively in receptor-mediated uptake of extracellular molecules, including lipoproteins and proteases. This article reviews recent work that indicates that LRP1 is phosphorylated on both serine and tyrosine residues. Tyrosine-phosphorylated LRP1 is specifically associated with the cellular docking protein Shc. The results suggest that ligand internalization by LRP1 is regulated by phosphorylation. In addition, LRP1 is now, like several of its close relatives, implicated in signal transduction. [PUBMED: 12069755] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.