Results 251 to 260 of about 157,920 (289)

New Functions for C2 Domains

Science Signaling, 2001
The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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Arabidopsis PLDs with C2‐domain function distinctively in hypoxia

Physiologia Plantarum, 2018
Hypoxia (oxygen deprivation) causes metabolic disturbances at physiological, biochemical and genetic levels and results in decreased plant growth and development. Phospholipase D (PLD)‐mediated signaling was reported for abiotic and biotic stress signaling events in plants.
Premkumar, Albert, Lindberg, Sylvia, Lager, Ida, Rasmussen, Ulla, Schulz, Alexander   +4 more
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Roles of calcium ions in the membrane binding of C2 domains

Biochemical Journal, 2001
The C2 domain is a membrane-targeting domain found in many cellular proteins involved in signal transduction or membrane trafficking. The majority of C2 domains co-ordinate multiple Ca2+ ions and bind the membrane in a Ca2+-dependent manner. To understand the mechanisms by which Ca2+ mediates the membrane binding of C2 domains, we measured the membrane
R V, Stahelin, W, Cho
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Otoferlin: a multi-C2 domain protein essential for hearing

Trends in Neurosciences, 2012
Sound is encoded at synapses between cochlear inner hair cells and the auditory nerve. These synapses are anatomically and functionally specialized to transmit acoustic information with high fidelity over a lifetime. The molecular mechanisms of hair-cell transmitter release have recently attracted substantial interest.
Tina, Pangršič, Ellen, Reisinger, Tobias, Moser   +2 more
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Crystal structure of human Intersectin-2L C2 domain

Biochemical and Biophysical Research Communications, 2013
Intersectin-2L (ITSN-2L) is a long isoform of ITSN family, which is a multimodule scaffolding protein functioning in membrane-associated molecular trafficking and signal transduction pathways. ITSN-2L possesses a carboxy-terminal extension encoding a Dbl homology domain (DH), a pleckstrin homology domain (PH) and a C2 domain, suggesting that it could ...
Wei, Zhang, Yang, Shen, Guomei, Xiong, Yahong, Guo, Lingfu, Deng, Bing, Li, Jihong, Yang, Chao, Qi   +7 more
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DOC2B, C2 Domains, and Calcium: A Tale of Intricate Interactions

Molecular Neurobiology, 2010
Ca(+2)-dependent exocytosis involves vesicle docking, priming, fusion, and recycling. This process is performed and regulated by a vast number of synaptic proteins and depends on proper protein-protein and protein-lipid interactions. Double C2 domain (DOC2) is a protein family of three isoforms found while screening DNA libraries with a C2 probe.
Reut, Friedrich, Adva, Yeheskel, Uri, Ashery   +2 more
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Hemophilic factor VIII C1- and C2-domain missense mutations and their modeling to the 1.5-angstrom human C2-domain crystal structure

Blood, 2000
AbstractFactor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized to the high-resolution C2 structure and to a homology model of C1.
M L, Liu, B W, Shen, S, Nakaya, K P, Pratt, K, Fujikawa, E W, Davie, B L, Stoddard, A R, Thompson   +7 more
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The AD3 locus of synaptotagmin-1 C2 domains modulates domain stability

Biophysical Journal
Synaptotagmin-1 (syt1) functions as the Ca2+-dependent sensor that triggers the rapid and synchronous release of neurotransmitters from neurotransmitter-containing vesicles during neuronal exocytosis. The syt1 protein has two homologous tandem C2 domains that interact with phospholipids in a Ca2+-dependent manner.
Matthew J, Dominguez, Anthony A, Bui, Johanna, Villarreal, Adam, Snow, Souvic, Karmakar, Faraz M, Harsini, Patrick J, Rock, Anne M, Rice, Kerry L, Fuson, R Bryan, Sutton   +9 more
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Characterization of a novel C. elegans RGS protein with a C2 domain: evidence for direct association between C2 domain and Gαq subunit

Life Sciences, 2003
RGS (regulator of G protein signaling) proteins are GTPase-activating proteins (GAPs) for heterotrimeric G protein alpha subunits and negatively regulate G protein-mediated signal transduction. In this study, we determined the cDNA sequence of a novel Caenorhabditis elegans (C. elegans) RGS protein. The predicted protein, termed C2-RGS, consists of 782
Motoko, Sato, Kayoko, Moroi, Mariko, Nishiyama, Jing, Zhou, Hirokazu, Usui, Yoshitoshi, Kasuya, Mitsunori, Fukuda, Yuji, Kohara, Issei, Komuro, Sadao, Kimura   +9 more
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The C-Terminal Domain of Pancreatic Lipase: Functional and Structural Analogies with C2 Domains

Current Protein & Peptide Science, 2000
The 3D structure of pancreatic lipase (PL) consists of two functional domains. The N-terminal domain belongs to the alpha/beta hydrolase fold and contains the active site, which involves a catalytic triad analogous to that present in serine proteases. The beta-sandwich C-terminal domain of PL plays an important part in the binding process between the ...
H, Chahinian, B, Sias, F, Carrière
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