Interaction of members of the heat shock protein-70 family with the macrophage mannose receptor

Journal of Leukocyte Biology

Seungchan Yang¹  David J. Vigerust,  and¹  Virginia L. Shepherd, ¹ 

[1] Departments of  Veterans Affairs Medical Center and Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, Tennessee, USA

关键词: receptor;    binding proteins;    cytoplasmic tail;   

DOI  :  10.1189/jlb.1111562

学科分类：生理学

来源: Federation of American Societies for Experimental Biology

【 摘 要 】

The macrophage MR has been the subject of investigation for over 20 years, and several important physiological functions have been described. However, the molecular mechanisms that regulate MR signaling and trafficking during these processes still remain elusive. The focus of the current paper was to identify potential cellular MR-interacting proteins. An initial screen of binding proteins in MR-expressing cells was performed using coimmunoprecipitation, followed by identification of matching peptide sequences using proteomics and MS. The major class of binding proteins identified belonged to the heat shock family of proteins. The specific interaction of the MR with HSP70 family members was validated by Western blot analysis, ligand binding assays, and intracellular colocalization using confocal microscopy. Additional studies indicated that inhibition of the HSP BiP by treatment of cells with EGCG reduced BiP interaction with and surface expression of the MR. Studies of possible motifs within the cytoplasmic tail of the receptor suggested that a juxtamembrane dibasic sequence may contribute to the interaction with BiP. These findings suggest that the molecular association of the MR with HSP70 family members via the receptor cytoplasmic tail may contribute to MR trafficking in macrophages.

【 授权许可】

Unknown