Molecular basis for the interaction of low density lipoprotein receptor-related protein 1 (LRP1) with integrin alphaMbeta2: identification of binding sites within alphaMbeta2 for LRP1.

ABSTRACT: The LDL receptor-related protein 1 (LRP1) is a large endocytic receptor that controls macrophage migration in part by interacting with β(2) integrin receptors. However, the molecular mechanism underlying LRP1 integrin recognition is poorly understood. Here, we report that LRP1 specifically recognizes α(M)β(2) but not its homologous receptor α(L)β(2). The interaction between these two cellular receptors in macrophages is significantly enhanced upon α(M)β(2) activation by LPS and is mediated by multiple regions in both LRP1 and α(M)β(2). Specifically, we find that both the heavy and light chains of LRP1 are involved in α(M)β(2) binding. Within the heavy chain, the binding is mediated primarily via the second and fourth ligand binding repeats. For α(M)β(2), we find that the α(M)-I domain repr

SUBMITTER: Ranganathan S 

PROVIDER: S-EPMC3162413 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature