Endocytosis of GABAC receptors depends on subunit composition and is regulated by protein kinase C-ζ and protein phosphatase 1

2015 ◽  
Vol 134 (2) ◽  
pp. 233-246 ◽  
Author(s):  
Lisa Linck ◽  
Jasmin Binder ◽  
Christian Haynl ◽  
Ralf Enz
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Subunit Composition ◽  
Kinase C ◽  
Gabac Receptors

Regulation of Choline Transporter Surface Expression and Phosphorylation by Protein Kinase C and Protein Phosphatase 1/2A

2004 ◽  
Vol 310 (2) ◽  
pp. 536-545 ◽  
Author(s):  
Jeremiah Gates ◽  
Shawn M. Ferguson ◽  
Randy D. Blakely ◽  
Subbu Apparsundaram
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Surface Expression ◽  
Protein Phosphatase 1 ◽  
Choline Transporter ◽  
Kinase C

scholarly journals Protein Kinase C-induced Activation of a Ceramide/Protein Phosphatase 1 Pathway Leading to Dephosphorylation of p38 MAPK

2006 ◽  
Vol 281 (48) ◽  
pp. 36793-36802 ◽  
Author(s):  
Kazuyuki Kitatani ◽  
Jolanta Idkowiak-Baldys ◽  
Jacek Bielawski ◽  
Tarek A. Taha ◽  
Russell W. Jenkins ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
P38 Mapk ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Kinase C

A Novel Protein Phosphatase-1 Inhibitory Protein Potentiated by Protein Kinase C. Isolation from Porcine Aorta Media and Characterization1

1995 ◽  
Vol 118 (6) ◽  
pp. 1104-1107 ◽  
Author(s):  
Masumi Eto ◽  
Toshihiro Ohmori ◽  
Masashi Suzuki ◽  
Kenji Furuya ◽  
Fumi Morita
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Protein Phosphatase 1 ◽  
Inhibitory Protein ◽  
Kinase C ◽  
Novel Protein

Overexpression of HSP‐70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity

1998 ◽  
Vol 12 (6) ◽  
pp. 451-459 ◽  
Author(s):  
Xuan Z. Ding ◽  
George C. Tsokos ◽  
Juliann G. Kiang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Hsp 70 ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Inhibiting Protein

scholarly journals Mechanisms of desensitization of the adrenocorticotropin response to arginine vasopressin in ovine anterior pituitary cells

2005 ◽  
Vol 184 (1) ◽  
pp. 29-40 ◽  
Author(s):  
A Hassan ◽  
D Mason
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Anterior Pituitary ◽  
Receptor Internalization ◽  
Pituitary Cells ◽  
Acth Secretion ◽  
Kinase C ◽  
Anterior Pituitary Cells ◽  
Vasopressin Receptors

Arginine vasopressin (AVP) stimulates adrenocorticotropin (ACTH) secretion from corticotroph cells of the anterior pituitary via activation of the V1b vasopressin receptor, a member of the G protein-coupled receptor (GPCR) family. Recently, we have shown that treatment of ovine anterior pituitary cells with AVP for short periods results in reduced responsiveness to subsequent stimulation with AVP. The aim of this study was to investigate mechanisms involved in this desensitization process. Among the GPCR family, rapid desensitization is commonly mediated by receptor phosphorylation, with resensitization being mediated by internalization and subsequent dephosphorylation of the receptors by protein phosphatases. Since desensitization of V1a vasopressin receptors is mediated by protein kinase C-mediated receptor phosphorylation, we investigated the involvement of this enzyme in desensitization of the ACTH response to AVP. Treatment of perifused ovine anterior pituitary cells with the specific protein kinase C (PKC) activator 1,2-dioctanoyl-sn-glycerol (300 μM) did not induce any reduction in response to a subsequent 5-min stimulation with 100 nM AVP, despite potently stimulating ACTH secretion. Likewise, the results obtained using the PKC inhibitor Ro 31-8220 were not consistent with involvement of PKC in AVP desensitization: 2 μM Ro 31-8220 did not reduce the ability of a 10 nM AVP pretreatment to induce desensitization to a subsequent stimulation with 100 nM AVP. Pharmacologic blockade of receptor internalization by treatment with 0.25 mg/ml concanavalin A significantly impaired the ability of a 15-min pretreatment with 10 nM AVP to induce desensitization, rather than affecting resensitization. Treatment with 10 nM okadaic acid, an inhibitor of protein phosphatase 1 and 2A, had no effect on either resensitization or desensitization. In contrast, inhibition of protein phosphatase 2B (PP2B) with 1 μM FK506 decreased the rate of resensitization: complete recovery from desensitization took 40 min, whereas in controls recovery was complete 20 min after termination of the pretreatment. These results indicate that desensitization of the ACTH response to AVP is not mediated by PKC-catalyzed phosphorylation, suggesting subtype-specific differences in the regulation of V1a and V1b vasopressin receptors. The data demonstrate that desensitization was dependent, at least in part, upon receptor internalization and that resensitization was dependent upon PP2B-mediated receptor dephosphorylation.

Phosphorylation of the Protein Phosphatase Type 1 Inhibitor Protein CPI-17 by Protein Kinase C

2007 ◽  
pp. 209-224 ◽  
Author(s):  
Michael P. Walsh ◽  
Marija Susnjar ◽  
Jingti Deng ◽  
Cindy Sutherland ◽  
Eniko Kiss ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphatase ◽  
Inhibitor Protein ◽  
Kinase C ◽  
Protein Phosphatase Type 1 ◽  
Protein Phosphatase Type

scholarly journals Protein kinase C inhibits GABAC receptors independent of consensus phosphorylation sites in the second intracellular loop

1997 ◽  
Vol 73 ◽  
pp. 160
Author(s):  
Manahu Sakurai ◽  
Koii Hatama ◽  
Tadashi Kusama ◽  
Yasuo Kizawa ◽  
George R Uhl ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphorylation Sites ◽  
Intracellular Loop ◽  
Kinase C ◽  
Gabac Receptors
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