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The c2 domain calcium-binding motif investing

Октябрь 2, 2012

the c2 domain calcium-binding motif investing

Human cPLA 2α gene was cloned via RT-PCR followed by site-directed mutagenesis to construct Calcium-binding C2 domain cells lost the ability of membrane. C2 domain (C2B) binds calcium and anionic phospholipids with a Of the six well-defined protein domains of Munc/2, C2B. phagocytosis, suggesting that C2 domain membrane binding mology domain ; BAR, bin-amphiphysin-Rvs; CBL, calcium binding. GPS FOREX ROBOT 2022 MOVIE

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Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Functional diversity of C2 domains of synaptotagmin family. Mutational analysis of inositol high polyphosphate binding domain. A putative Ras GTPase activating protein acts as a negative regulator of signaling by the Sevenless receptor tyrosine kinase. Biochem J. Kinetic analysis of a high molecular weight phospholipase A2 from rat kidney: divalent metal-dependent trapping of enzyme on product-containing vesicles.

C2 domain conformational changes in phospholipase C-delta 1. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. Phosphatidylinositol 3-kinase: structure and expression of the kd catalytic subunit. The rsp5-domain is shared by proteins of diverse functions.

Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p Mol Cell Biol. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody. Localization of phosphatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarboxylase.

Calcium binding and conformational response in EF-hand proteins. Synaptic vesicles and exocytosis. Annu Rev Neurosci. Calcium-binding proteins 1: EF-hands. Protein Profile. Localization of synaptotagmin-binding domains on syntaxin. J Neurosci. Neural transmission. Synaptotagmin is just a calcium sensor.

Curr Biol. Cloning and expression of multiple protein kinase C cDNAs. Phospholipase C isozymes: structural and functional similarities. Ciba Found Symp. Identification of a set of genes with developmentally down-regulated expression in the mouse brain.

Biochem Biophys Res Commun. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Structure and function of human perforin. Determinants that govern high-affinity calcium binding. Adv Second Messenger Phosphoprotein Res. A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction.

A novel mammalian Ras GTPase-activating protein which has phospholipid-binding and Btk homology regions. A second gene product of the inositol-phospholipid-specific phospholipase C delta subclass. Localization of protein kinases by anchoring proteins: a theme in signal transduction. A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C.

Protein kinase C. Seeing two domains. Protein kinase C: structure, function, and regulation. Synaptotagmin is an inositol polyphosphate binding protein: isolation and characterization as an Ins 1,3,4,5-P4 binding protein. The molecular heterogeneity of protein kinase C and its implications for cellular regulation.

Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Protein kinase C and lipid signaling for sustained cellular responses. EMBO J. Synaptic function is impaired but not eliminated in C. Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing.

Cloning of rat brain protein kinase C complementary DNA. Doc2: a novel brain protein having two repeated C2-like domains. Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1. Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family.

Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. The complete primary structure of protein kinase C--the major phorbol ester receptor. Intracellular signalling. SH2 and SH3 domains: from structure to function. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C.

Redistribution of 5-lipoxygenase and cytosolic phospholipase A2 to the nuclear fraction upon macrophage activation. Regulation of inositol phospholipid-specific phospholipase C isozymes. Studies of inositol phospholipid-specific phospholipase C. For example, the mechanical activity of cardiac and skeletal muscle often leads to tears and disruptions of the plasma membrane 1—4.

In response to membrane disruption, an elaborate membrane repair system is found in many types of cells that reseals the membrane and prevents cell death. In support of this, dysferlin-null mice are unable to exclude fluorescent dyes from entering muscle tissue after wounding, and dysferlin knockdown zebrafish are deficient in their ability to repair sarcolemma lesions 6— In humans, mutations in dysferlin have been linked to a group of muscular dystrophies known as dysferlinopathies that are characterized by muscle atrophy and increased amounts of adipose tissue 11— Beyond muscle, dysferlin is expressed at lower levels in several other cell types, including monocytes, where it may regulate cell adhesion and chemotaxis 19— Dysferlin is one member of the ferlin family of proteins.

First characterized in Caenorhabditis elegans, ferlin proteins are composed of multiple N-terminal C2 domains followed by a C-terminal single-pass transmembrane region Fig. Dysferlin possesses seven C2 domains and typically resides on the sarcolemma membrane, although it has also been detected on intracellular vesicles 23, Analysis of the dysferlin sequence indicates that although C2 domains at the C-terminus share the conserved five conserved aspartates, C2 domains at the N-terminus show fewer conserved aspartates, with only three aspartates in the loops of the C2A domain

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