Non-receptor activators of heterotrimeric G-protein signaling (AGS proteins).
*Signal Transduction; Animals; Biological; G-Protein-Coupled/*metabolism; Heterotrimeric GTP-Binding Proteins/*metabolism; Humans; Models; Receptors
G-protein coupled receptor (GPCR) signaling represents one of the most conserved and ubiquitous means in mammalian cells for transferring information across the plasma membrane to the intracellular environment. Heterotrimeric G-protein subunits play key roles in transducing these signals, and intracellular regulators influencing the activation state and interaction of these subunits regulate the extent and duration of GPCR signaling. One class of intracellular regulator, the non-receptor activators of G-protein signaling (or AGS proteins), are the major focus of this review. AGS proteins provide a basis for understanding the function of heterotrimeric G-proteins in both GPCR-driven and GPCR independent cellular signaling pathways.
Cismowski Mary J
Seminars in cell & developmental biology
2006
2006-06
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1016/j.semcdb.2006.03.003" target="_blank" rel="noreferrer noopener">10.1016/j.semcdb.2006.03.003</a>
HSV-2 ICP34.5 protein modulates herpes simplex virus glycoprotein processing.
*Protein Processing; Animals; Cercopithecus aethiops; Cloning; Gene Expression; Herpesvirus 1; Herpesvirus 2; Human/*genetics; Molecular; Post-Translational; Vero Cells; Viral Envelope Proteins/*metabolism; Viral Proteins/genetics/*metabolism
The ICP34.5 gene from HSV-2 strain 333 was cloned and, when expressed in Vero cells, enhanced the efficiency and extent of glycoprotein processing of glycoprotein C (gC1), a representative viral glycoprotein, during infection with
Chatterjee Somik; Wang Jason W; Cismowski Mary J; Bower John R; Rosenthal Kenneth Steven
Archives of virology
2009
1905-07
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
<a href="http://doi.org/10.1007/s00705-009-0341-9" target="_blank" rel="noreferrer noopener">10.1007/s00705-009-0341-9</a>