4.7 Article

Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin

Journal

BLOOD
Volume 112, Issue 13, Pages 5212-5218

Publisher

AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2008-03-146068

Keywords

-

Categories

Funding

  1. National Institutes of Health [DK56267, DK26263, DK32094, HL31579]
  2. National Health Service Research and Development Directorate (United Kingdom)
  3. Director, Office of Health and Environment Research Division, US Department of Energy [DE-AC03-76SF00098]

Ask authors/readers for more resources

The Lutheran (Lu) and Lu(v13) blood group glycoproteins function as receptors for extracellular matrix laminins. Lu and Lu( v13) are linked to the erythrocyte cytoskeleton through a direct interaction with spectrin. However, neither the molecular basis of the interaction nor its functional consequences have previously been delineated. In the present study, we defined the binding motifs of Lu and Lu( v13) on spectrin and identified a functional role for this interaction. We found that the cytoplasmic domains of both Lu and Lu( v13) bound to repeat 4 of the alpha spectrin chain. The interaction of full-length spectrin dimer to Lu and Lu( v13) was inhibited by repeat 4 of alpha-spectrin. Further, resealing of this repeat peptide into erythrocytes led to weakened Lu-cytoskeleton interaction as demonstrated by increased detergent extractability of Lu. Importantly, disruption of the Lu-spectrin linkage was accompanied by enhanced cell adhesion to laminin. We conclude that the interaction of the Lu cytoplasmic tail with the cytoskeleton regulates its adhesive receptor function.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available