scholarly journals A cell-free method for expressing and reconstituting membrane proteins enables functional characterization of the plant receptor-like protein kinase FERONIA

2017 ◽  
Vol 292 (14) ◽  
pp. 5932-5942 ◽  
Author(s):  
Benjamin B. Minkoff ◽  
Shin-ichi Makino ◽  
Miyoshi Haruta ◽  
Emily T. Beebe ◽  
Russell L. Wrobel ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Membrane Proteins ◽  
Functional Characterization ◽  
A Cell

scholarly journals Identification and functional characterization of protein kinase C isozymes in platelets and HEL cells.

1992 ◽  
Vol 267 (14) ◽  
pp. 10011-10017
Author(s):  
J Grabarek ◽  
M Raychowdhury ◽  
K Ravid ◽  
K.C. Kent ◽  
P.J. Newman ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Functional Characterization ◽  
Kinase C ◽  
Hel Cells

scholarly journals Cloning and functional characterization of the human fractalkine receptor promoter regions

2002 ◽  
Vol 368 (3) ◽  
pp. 753-760 ◽  
Author(s):  
Alexandre GARIN ◽  
Philippe PELLET ◽  
Philippe DETERRE ◽  
Patrice DEBRÉ ◽  
Christophe COMBADIÈRE
Keyword(s):  
Functional Characterization ◽  
Cell Types ◽  
Promoter Regions ◽  
Exon 2 ◽  
Reading Frame ◽  
Fractalkine Receptor ◽  
A Cell ◽  
Exon 4 ◽  
Coronary Events

We have previously shown that reduced expression of the fractalkine receptor, CX3CR1, is correlated with rapid HIV disease progression and with reduced susceptibility to acute coronary events. In order to elucidate the mechanisms underlying transcriptional regulation of CX3CR1 expression, we structurally and functionally characterized the CX3CR1 gene. It consists of four exons and three introns spanning over 18kb. Three transcripts are produced by splicing the three untranslated exons with exon 4, which contains the complete open reading frame. The transcript predominantly found in leucocytes corresponds to the splicing of exon 2 with exon 4. Transcripts corresponding to splicing of exons 1 and 4 are less abundant in leucocytes and splicing of exons 3 and 4 are rare longer transcripts. A constitutive promoter activity was found in the regions extending upstream from untranslated exons 1 and 2. Interestingly, exons 1 and 2 enhanced the activity of their respective promoters in a cell-specific manner. These data show that the CX3CR1 gene is controlled by three distinct promoter regions, which are regulated by their respective untranslated exons and that lead to the transcription of three mature messengers. This highly complex regulation may allow versatile and precise expression of CX3CR1 in various cell types.

Functional characterization of an adhesive component from the embryonic chick neural retina

1979 ◽  
Vol 36 (1) ◽  
pp. 323-342
Author(s):  
R. Rutz ◽  
J. Lilien
Keyword(s):  
Conditioned Medium ◽  
Ph Dependence ◽  
Functional Characterization ◽  
Surface Binding ◽  
Cell Agglutination ◽  
Tissue Specific ◽  
A Cell ◽  
Surface Ligand ◽  
Fixed Cell

We have developed a quantitative assay for tissue-specific adhesive components which is based on the agglutination of glutaraldehyde-fixed cells. At least 2 components are required for fixed-cell agglutination: a cell-surface ligand which is obtained from tissue culture-conditioned medium, and a soluble ‘agglutinin’ which accumulates in conditioned medium from monolayer cultures. Our results suggest that the surface-binding ligand and the agglutinin interact directly, resulting in tissue-specific agglutination of cells. The agglutination reaction exhibits divalent cation, temperature, and pH dependence. Several models of cell adhesion are described; the simplest of these which can account for the data is a multicomponent model in which the 2 adhesive components have structural roles.

Biochemical and functional characterization of the ROC domain of DAPK establishes a new paradigm of GTP regulation in ROCO proteins

2012 ◽  
Vol 40 (5) ◽  
pp. 1052-1057 ◽  
Author(s):  
Shani Bialik ◽  
Adi Kimchi
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Functional Characterization ◽  
Leucine Rich Repeat ◽  
New Paradigm ◽  
Gtp Binding ◽  
Death Associated Protein Kinase ◽  
In Cis ◽  
Leucine Rich Repeat Protein

DAPK (death-associated protein kinase) is a newly recognized member of the mammalian family of ROCO proteins, characterized by common ROC (Ras of complex proteins) and COR (C-terminal of ROC) domains. In the present paper, we review our recent work showing that DAPK is functionally a ROCO protein; its ROC domain binds and hydrolyses GTP. Furthermore, GTP binding regulates DAPK catalytic activity in a novel manner by enhancing autophosphorylation on inhibitory Ser308, thereby promoting the kinase ‘off’ state. This is a novel mechanism for in cis regulation of kinase activity by the distal ROC domain. The functional similarities between DAPK and the Parkinson's disease-associated protein LRRK2 (leucine-rich repeat protein kinase 2), another member of the ROCO family, are also discussed.

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

scholarly journals Functional Characterization of the Interaction of Ste50p with Ste11p MAPKKK inSaccharomyces cerevisiae

1999 ◽  
Vol 10 (7) ◽  
pp. 2425-2440 ◽  
Author(s):  
Cunle Wu ◽  
Ekkehard Leberer ◽  
David Y. Thomas ◽  
Malcolm Whiteway
Keyword(s):  
Protein Kinase ◽  
Functional Characterization ◽  
Hog Pathway ◽  
C Terminus ◽  
Extracellular Signal ◽  
Osmotic Stress Response ◽  
N Terminus

The Saccharomyces cerevisiae Ste11p protein kinase is a homologue of mammalian MAPK/extracellular signal-regulated protein kinase kinase kinases (MAPKKKs or MEKKs) as well as theSchizosaccharomyces pombe Byr2p kinase. Ste11p functions in several signaling pathways, including those for mating pheromone response and osmotic stress response. The Ste11p kinase has an N-terminal domain that interacts with other signaling molecules to regulate Ste11p function and direct its activity in these pathways. One of the Ste11p regulators is Ste50p, and Ste11p and Ste50p associate through their respective N-terminal domains. This interaction relieves a negative activity of the Ste11p N terminus, and removal of this negative function is required for Ste11p function in the high-osmolarity glycerol (HOG) pathway. The Ste50p/Ste11p interaction is also important (but not essential) for Ste11p function in the mating pathway; in this pathway binding of the Ste11p N terminus with both Ste50p and Ste5p is required, with the Ste5p association playing the major role in Ste11p function. In vitro, Ste50p disrupts an association between the catalytic C terminus and the regulatory N terminus of Ste11p. In addition, Ste50p appears to modulate Ste11p autophosphorylation and is itself a substrate of the Ste11p kinase. Therefore, both in vivo and in vitro data support a role for Ste50p in the regulation of Ste11p activity.

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