scholarly journals Putative calcium-binding domains of theCaenorhabditis elegansBK channel are dispensable for intoxication and ethanol activation

2015 ◽  
Vol 14 (6) ◽  
pp. 454-465 ◽  
Author(s):  
S. J. Davis ◽  
L. L. Scott ◽  
G. Ordemann ◽  
A. Philpo ◽  
J. Cohn ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Binding Domains

S100A13 and S100A6 exhibit distinct translocation pathways in endothelial cells

2002 ◽  
Vol 115 (15) ◽  
pp. 3149-3158 ◽  
Author(s):  
Hsiao-Ling Hsieh ◽  
Beat W. Schäfer ◽  
Jos A. Cox ◽  
Claus W. Heizmann
Keyword(s):  
Endothelial Cells ◽  
Calcium Binding ◽  
Protein Translocation ◽  
S100 Proteins ◽  
Cellular Functions ◽  
Specific Expression ◽  
Binding Domains ◽  
Cellular Environment ◽  
Ef Hands ◽  
Physiological Tasks

S100 proteins have attracted great interest in recent years because of their cell- and tissue-specific expression and association with various human pathologies. Most S100 proteins are small acidic proteins with calcium-binding domains — the EF hands. It is thought that this group of proteins carry out their cellular functions by interacting with specific target proteins, an interaction that is mainly dependent on exposure of hydrophobic patches, which result from calcium binding. S100A13, one of the most recently identified members of the S100 family, is expressed in various tissues. Interestingly,hydrophobic exposure was not observed upon calcium binding to S100A13 even though the dimeric form displays two high- and two low- affinity sites for calcium. Here, we followed the translocation of S100A13 in response to an increase in intracellular calcium levels, as protein translocation has been implicated in assembly of signaling complexes and signaling cascades, and several other S100 proteins are involved in such events. Translocation of S100A13 was observed in endothelial cells in response to angiotensin II, and the process was dependent on the classic Golgi-ER pathway. By contrast, S100A6 translocation was found to be distinct and dependent on actin-stress fibers. These experiments suggest that different S100 proteins utilize distinct translocation pathways, which might lead them to certain subcellular compartments in order to perform their physiological tasks in the same cellular environment.

scholarly journals Two Structural Motifs within Canonical EF-Hand Calcium-Binding Domains Identify Five Different Classes of Calcium Buffers and Sensors

PLoS ONE ◽  
2014 ◽  
Vol 9 (10) ◽  
pp. e109287 ◽  
Author(s):  
Konstantin Denessiouk ◽  
Sergei Permyakov ◽  
Alexander Denesyuk ◽  
Eugene Permyakov ◽  
Mark S. Johnson
Keyword(s):  
Calcium Binding ◽  
Structural Motifs ◽  
Binding Domains ◽  
Ef Hand ◽  
Calcium Buffers

scholarly journals Evolutionary perspective on annexin calcium-binding domains

2004 ◽  
Vol 1742 (1-3) ◽  
pp. 133-140 ◽  
Author(s):  
R.O. Morgan ◽  
S. Martin-Almedina ◽  
J.M. Iglesias ◽  
M.I. Gonzalez-Florez ◽  
M.P. Fernandez
Keyword(s):  
Calcium Binding ◽  
Evolutionary Perspective ◽  
Binding Domains

scholarly journals Expression and Functional Characteristics of Calpain 3 Isoforms Generated through Tissue-Specific Transcriptional and Posttranscriptional Events

1999 ◽  
Vol 19 (6) ◽  
pp. 4047-4055 ◽  
Author(s):  
Muriel Herasse ◽  
Yasuko Ono ◽  
Françoise Fougerousse ◽  
Ei-ichi Kimura ◽  
Daniel Stockholm ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Calcium Binding ◽  
Biochemical Properties ◽  
Therapeutic Strategies ◽  
Biological Functions ◽  
Truncated Protein ◽  
Binding Domains ◽  
Calpain 3 ◽  
Its Gene ◽  
Proteolytic Activities

ABSTRACT Calpain 3 is a nonlysosomal cysteine protease whose biological functions remain unknown. We previously demonstrated that this protease is altered in limb girdle muscular dystrophy type 2A patients. Preliminary observations suggested that its gene is subjected to alternative splicing. In this paper, we characterize transcriptional and posttranscriptional events leading to alterations involving the NS, IS1, and IS2 regions and/or the calcium binding domains of the mouse calpain 3 gene (capn3). These events can be divided into three groups: (i) splicing of exons that preserve the translation frame, (ii) inclusion of two distinct intronic sequences between exons 16 and 17 that disrupt the frame and would lead, if translated, to a truncated protein lacking domain IV, and (iii) use of an alternative first exon specific to lens tissue. In addition, expression of these isoforms seems to be regulated. Investigation of the proteolytic activities and titin binding abilities of the translation products of some of these isoforms clearly indicated that removal of these different protein segments affects differentially the biochemical properties examined. In particular, removal of exon 6 impaired the autolytic but not fodrinolytic activity and loss of exon 16 led to an increased titin binding and a loss of fodrinolytic activity. These results are likely to impact our understanding of the pathophysiology of calpainopathies and the development of therapeutic strategies.

High-level expression in Escherichia coli of calcium-binding domains of an embryonic sea urchin protein

Gene ◽  
1984 ◽  
Vol 31 (1-3) ◽  
pp. 155-164 ◽  
Author(s):  
Mark Muesing ◽  
Clifford D. Carpenter ◽  
William H. Klein ◽  
Barry Polisky
Keyword(s):  
Escherichia Coli ◽  
Sea Urchin ◽  
Calcium Binding ◽  
High Level Expression ◽  
Expression In Escherichia Coli ◽  
Binding Domains ◽  
High Level

scholarly journals Molecular basis of the 14-3-3 protein-dependent activation of yeast neutral trehalase Nth1

2017 ◽  
Vol 114 (46) ◽  
pp. E9811-E9820 ◽  
Author(s):  
Miroslava Alblova ◽  
Aneta Smidova ◽  
Vojtech Docekal ◽  
Jan Vesely ◽  
Petr Herman ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Complex Structure ◽  
Scaffolding Proteins ◽  
Fluorescence Studies ◽  
Binding Domains ◽  
Distinct Structure ◽  
Allosteric Effector ◽  
Flexible Part ◽  
Client Proteins ◽  
Partner Proteins

The 14-3-3 proteins, a family of highly conserved scaffolding proteins ubiquitously expressed in all eukaryotic cells, interact with and regulate the function of several hundreds of partner proteins. Yeast neutral trehalases (Nth), enzymes responsible for the hydrolysis of trehalose to glucose, compared with trehalases from other organisms, possess distinct structure and regulation involving phosphorylation at multiple sites followed by binding to the 14-3-3 protein. Here we report the crystal structures of yeast Nth1 and its complex with Bmh1 (yeast 14-3-3 isoform), which, together with mutational and fluorescence studies, indicate that the binding of Nth1 by 14-3-3 triggers Nth1’s activity by enabling the proper 3D configuration of Nth1’s catalytic and calcium-binding domains relative to each other, thus stabilizing the flexible part of the active site required for catalysis. The presented structure of the Bmh1:Nth1 complex highlights the ability of 14-3-3 to modulate the structure of a multidomain binding partner and to function as an allosteric effector. Furthermore, comparison of the Bmh1:Nth1 complex structure with those of 14-3-3:serotonin N-acetyltransferase and 14-3-3:heat shock protein beta-6 complexes revealed similarities in the 3D structures of bound partner proteins, suggesting the highly conserved nature of 14-3-3 affects the structures of many client proteins.

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