Atypical Porcine Type I Interferon. Biochemical and Biological Characterization of the Recombinant Protein Expressed in Insect Cells

1995 ◽  
Vol 230 (1) ◽  
pp. 200-206 ◽  
Author(s):  
Ping-De Niu ◽  
Francois Lefevre ◽  
Dominique Mege ◽  
Claude Bonnardiere
Cytokine ◽  
2010 ◽  
Vol 52 (1-2) ◽  
pp. 63
Author(s):  
Steven Carbone ◽  
Sidney Pestka ◽  
Ronald G. Jubin

2010 ◽  
Vol 30 (2) ◽  
pp. 81-88 ◽  
Author(s):  
Qinghua Xue ◽  
Limin Yang ◽  
Xiaoling Liu ◽  
Wenjun Liu

Cytokine ◽  
2008 ◽  
Vol 43 (3) ◽  
pp. 329
Author(s):  
Angela Walker ◽  
R. Michael Roberts
Keyword(s):  
Type I ◽  

2012 ◽  
Vol 33 (4) ◽  
pp. 886-898 ◽  
Author(s):  
Qiang Wan ◽  
W.D. Niroshana Wicramaarachchi ◽  
Ilson Whang ◽  
Bong-Soo Lim ◽  
Myung-Joo Oh ◽  
...  

2014 ◽  
Vol 94 ◽  
pp. 7-14 ◽  
Author(s):  
Sebastian A. Stifter ◽  
Jodee A. Gould ◽  
Niamh E. Mangan ◽  
Hugh H. Reid ◽  
Jamie Rossjohn ◽  
...  

2009 ◽  
Vol 29 (24) ◽  
pp. 6401-6412 ◽  
Author(s):  
Jianghuai Liu ◽  
Lucas P. Carvalho ◽  
Sabyasachi Bhattacharya ◽  
Christopher J. Carbone ◽  
K. G. Suresh Kumar ◽  
...  

ABSTRACT Phosphorylation of the degron of the IFNAR1 chain of the type I interferon (IFN) receptor triggers ubiquitination and degradation of this receptor and, therefore, plays a crucial role in negative regulation of IFN-α/β signaling. Besides the IFN-stimulated and Jak activity-dependent pathways, a basal ligand-independent phosphorylation of IFNAR1 has been described and implicated in downregulating IFNAR1 in response to virus-induced endoplasmic reticulum (ER) stress. Here we report purification and characterization of casein kinase 1α (CK1α) as a bona fide major IFNAR1 kinase that confers basal turnover of IFNAR1 and cooperates with ER stress stimuli to mediate phosphorylation-dependent degradation of IFNAR1. Activity of CK1α was required for phosphorylation and downregulation of IFNAR1 in response to ER stress and viral infection. While many forms of CK1 were capable of phosphorylating IFNAR1 in vitro, human CK1α and L-CK1 produced by the protozoan Leishmania major were also capable of increasing IFNAR1 degron phosphorylation in cells. Expression of leishmania CK1 in mammalian cells stimulated the phosphorylation-dependent downregulation of IFNAR1 and attenuated its signaling. Infection of mammalian cells with L. major modestly decreased IFNAR1 levels and attenuated cellular responses to IFN-α in vitro. We propose a role for mammalian and parasite CK1 enzymes in regulating IFNAR1 stability and type I IFN signaling.


Cytokine ◽  
2011 ◽  
Vol 56 (1) ◽  
pp. 23
Author(s):  
Sebastian A. Stifter ◽  
Kayee Fung ◽  
Niamh Mangan ◽  
Nicole de Weerd ◽  
Paul Hertzog
Keyword(s):  

1997 ◽  
Vol 272 (38) ◽  
pp. 23865-23870 ◽  
Author(s):  
Catherine M. Owczarek ◽  
Seung Y. Hwang ◽  
Kerry A. Holland ◽  
Lerna M. Gulluyan ◽  
Michael Tavaria ◽  
...  

2001 ◽  
Vol 108 (6) ◽  
pp. 459-466 ◽  
Author(s):  
Hirokazu Kashiwagi ◽  
Yoshiaki Tomiyama ◽  
Shuichi Nozaki ◽  
Teruo Kiyoi ◽  
Seiji Tadokoro ◽  
...  

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