Abstract:
:NK cells use surface NK receptors to discriminate self from non-self. The NK receptor ligand-binding domain (NKD) has been considered the sole regulator of ligand binding. Using a prototypic murine NK receptor, Ly49A, we show that the membrane proximal nonligand binding ecto-domain (the stalk region) is critical to ligand binding and signaling. The stalk region is required for receptor binding to ligand on target cells (trans interaction), but is dispensable for receptor binding to ligand on the same cell (cis interaction). Also, signaling in a trans manner depends on the stalk region mediating the formation of the immunological synapse. Thus, our data modeling receptor function at the cellular level reveal an essential role for the stalk region as a specific mediator of receptor signal integration, by which NKD-ligand interactions at the interface initiate and deliver information to the spatially separated cytoplasmic domain.
journal_name
Proc Natl Acad Sci U S Aauthors
Ito D,Iizuka YM,Katepalli MP,Iizuka Kdoi
10.1073/pnas.0900664106subject
Has Abstractpub_date
2009-07-07 00:00:00pages
11264-9issue
27eissn
0027-8424issn
1091-6490pii
0900664106journal_volume
106pub_type
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