Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
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DOI:
10.1074/jbc.273.4.2379
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发表时间:
1998-01-23
影响因子:
4.8
通讯作者:
Chang, DD
中科院分区:
文献类型:
--
作者:
Liliental, J;Chang, DD
The integrin beta subunit cytoplasmic domains are important for activation-dependent cell adhesion and adhesion-dependent signaling events. We report an interaction between integrin beta subunit cytoplasmic domain and Rack1, a Trp-Asp (WD) repeat protein that has been shown to bind activated protein kinase C, The Rack1-binding site on integrin beta(2) subunit resides within a conserved, membrane proximal region. In the yeast two-hybrid assay, WD repeats five to seven of Rack1 (Rack1-WD5/7) interact with integrin beta(1), beta(2), and beta(5) cytoplasmic domain, In eukaryotic cells, Rack1 co-immunoprecipitates with at least two different beta integrins, beta(1) integrins in 293T cells and beta(1) integrins in JY lymphoblastoid cells, Whereas Rack1-WD5/7 binds integrins constitutively, the association of full length Rack1 to integrins in vivo requires a treatment with phorbol esters, which promotes cell spreading and adhesion, These findings suggest that Rack1 may link protein kinase C directly to integrins and participate in the regulation of integrin functions.