English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Prolectin, a glycan-binding receptor on dividing B cells in germinal centers

MPS-Authors
There are no MPG-Authors in the publication available
External Resource
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Supplementary Material (public)
There is no public supplementary material available
Citation

Graham, S. A., Jégouzo, S. A. F., Yan, S., Powlesland, A. S., Brady, J. P., Taylor, M. E., et al. (2009). Prolectin, a glycan-binding receptor on dividing B cells in germinal centers. The Journal of Biological Chemistry, 284, 18537-18544. doi:10.1074/jbc.M109.012807.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0011-563E-5
Abstract
Prolectin, a previously undescribed glycan-binding receptor, has been identified by re-screening of the human genome for genes encoding proteins containing potential C-type carbohydrate-recognition domains. Glycan array analysis revealed that the carbohydrate-recognition domain in the extracellular domain of the receptor binds glycans with terminal α-linked mannose or fucose residues. Prolectin expressed in fibroblasts is found at the cell surface, but unlike many glycan-binding receptors it does not mediate endocytosis of a neoglycoprotein ligand. However, compared with other known glycan-binding receptors, the receptor contains an unusually large intracellular domain that consists of multiple sequence motifs, including phosphorylated tyrosine residues, that allow it to interact with signaling molecules such as Grb2. Immunohistochemistry has been used to demonstrate that prolectin is expressed on a specialized population of proliferating B cells in germinal centers. Thus, this novel receptor has the potential to function in carbohydrate-mediated communication between cells in the germinal center.