scholarly journals Identification of an alcohol binding site in the first cysteine-rich domain of protein kinase C δ

2006 ◽  
Vol 15 (9) ◽  
pp. 2107-2119 ◽  
Author(s):  
Joydip Das ◽  
Xiaojuan Zhou ◽  
Keith W. Miller
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Site ◽  
Rich Domain ◽  
Kinase C ◽  
Cysteine Rich Domain

scholarly journals The cysteine-rich domain of human proteins, neuronal chimaerin, protein kinase C and diacylglycerol kinase binds zinc. Evidence for the involvement of a zinc-dependent structure in phorbol ester binding

1991 ◽  
Vol 280 (1) ◽  
pp. 233-241 ◽  
Author(s):  
S Ahmed ◽  
R Kozma ◽  
J Lee ◽  
C Monfries ◽  
N Harden ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Hormone Receptors ◽  
Phorbol Esters ◽  
Steroid Hormone Receptors ◽  
Rich Domain ◽  
Kinase C ◽  
Cysteine Rich Domain

Diacylglycerol (DG) and its analogue phorbol 12-myristate 13-acetate (PMA) activate the ubiquitous phospholipid/Ca2(+)-dependent protein kinase, protein kinase C (PKC), and cause it to become tightly associated with membranes. DG is produced transiently as it is rapidly metabolized by DG kinase (DGK) to phosphatidic acid. Phorbol esters such as PMA are not metabolized and induced a prolonged membrane association of PKC. Until recently, PKC was the only known phorbol ester receptor. We have shown that a novel brain-specific cDNA, neuronal chimaerin (NC), expressed in Escherichia coli, binds phorbol ester with high affinity, stereospecificity and a phospholipid requirement [Ahmed, Kozma, Monfries, Hall, Lim, Smith & Lim (1990) Biochem. J. 272, 767-773]. The proteins NC, PKC and DGK possess a cysteine-rich domain with the motif HX11/12CX2CXnCX2CX4HX2CX6/7C (where n varies between 12 and 14). The partial motif, CX2CX13CX2C, is present in a number of transcription factors including the steroid hormone receptors and the yeast protein, GAL4, in which zinc plays a structural role of co-ordinating cysteine residues and is essential for DNA binding (protein-nucleic acid interactions). The cysteine-rich domain of NC and PKC is required for phospholipid-dependent phorbol is required for phospholipid-dependent phorbol ester binding, suggesting an involvement of this domain in protein-lipid interactions. We have expressed recombinant NC, PKC and DGK glutathione S-transferase and TrpE fusion proteins in E. coli to investigate the relationship between the cysteine-rich motif, HX11/12CX2CX10-14CX2CX4HX2CX6/7C, zinc and phorbol ester binding. The cysteine-rich domain of NC, PKC and DGK bound 65Zn2+ but only NC and PKC bound [3H]phorbol 12,13-dibutyrate. When NC and PKC were subjected to treatments known to remove metal ions from GAL4 and the human glucocorticoid receptor, phorbol ester binding was inhibited. These data provide evidence for the role of a zinc-dependent structure in phorbol ester binding.

Solution structure of a cysteine rich domain of rat protein kinase C

1994 ◽  
Vol 1 (6) ◽  
pp. 383-387 ◽  
Author(s):  
Ulrich Hommel ◽  
Mauro Zurini ◽  
Marcel Luyten
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Solution Structure ◽  
Rich Domain ◽  
Kinase C ◽  
Cysteine Rich Domain

scholarly journals Intracellular receptors for activated protein kinase C. Identification of a binding site for the enzyme

1991 ◽  
Vol 266 (23) ◽  
pp. 14866-14868
Author(s):  
D. Mochly-Rosen ◽  
H. Khaner ◽  
J. Lopez ◽  
B.L. Smith
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Site ◽  
Kinase C

scholarly journals RACK1 Regulates Integrin-mediated Adhesion, Protrusion, and Chemotactic Cell Migration via Its Src-binding Site

2003 ◽  
Vol 14 (2) ◽  
pp. 658-669 ◽  
Author(s):  
Elisabeth A. Cox ◽  
David Bennin ◽  
Ashley T. Doan ◽  
Timothy O'Toole ◽  
Anna Huttenlocher
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Site ◽  
Fluorescent Protein ◽  
Focal Adhesions ◽  
Expression Cloning ◽  
Chemotactic Migration ◽  
Cell Protrusion ◽  
Kinase C ◽  
Green Fluorescent

Mammalian cDNA expression cloning was used to identify novel regulators of integrin-mediated cell-substratum adhesions. Using a focal adhesion morphology screen, we identified a cDNA with homology to a receptor for activated protein kinase C (RACK1) that induced a loss of central focal adhesions and stress fibers in CHO-K1 cells. The identified cDNA was a C-terminal truncated form of RACK1 that had one of the putative protein kinase C binding sites but lacked the region proposed to bind the β integrin cytoplasmic domain and the tyrosine kinase Src. To investigate the role of RACK1 during cell spreading and migration, we tagged RACK1, a C-terminal truncated RACK1 and a point mutant that does not bind Src (RACK Y246F) with green fluorescent protein and expressed them in CHO-K1 cells. We found that RACK1 regulates the organization of focal adhesions and that it localizes to a subset of nascent focal complexes in areas of protrusion that contain paxillin but not vinculin. We also found that RACK1 regulates cell protrusion and chemotactic migration through its Src binding site. Together, these findings suggest that RACK1 regulates adhesion, protrusion, and chemotactic migration through its interaction with Src.

Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C

FEBS Letters ◽  
1997 ◽  
Vol 417 (2) ◽  
pp. 219-222 ◽  
Author(s):  
Jörg J Jacoby ◽  
Hans-Peter Schmitz ◽  
Jürgen J Heinisch
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Site ◽  
Yeast Protein ◽  
Kinase C

scholarly journals Structural and Functional Characterization of an Anesthetic Binding Site in the Second Cysteine-Rich Domain of Protein Kinase Cδ∗

2012 ◽  
Vol 103 (11) ◽  
pp. 2331-2340 ◽  
Author(s):  
Sivananthaperumal Shanmugasundararaj ◽  
Joydip Das ◽  
Warren S. Sandberg ◽  
Xiaojuan Zhou ◽  
Dan Wang ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Binding Site ◽  
Functional Characterization ◽  
Rich Domain ◽  
Cysteine Rich Domain ◽  
Protein Kinase Cδ
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