Journal ArticleDOI
The C2 Domains of Classical PKCs are Specific PtdIns(4,5)P2-sensing Domains with Different Affinities for Membrane Binding
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TLDR
Compared the three C2 domains of classical PKCs, it is shown that the plasma membrane dissociation event differed in each case, PKCalpha persisting for the longest time in the plasma membranes, followed by PKCgamma and, finally, PKCbeta, which probably reflects the different levels of Ca(2+) needed by each domain and their different affinities for PtdIns(4,5)P(2).About:
This article is published in Journal of Molecular Biology.The article was published on 2007-08-17. It has received 59 citations till now. The article focuses on the topics: C2 domain & Plasma protein binding.read more
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Survey of the year 2005: literature on applications of isothermal titration calorimetry.
TL;DR: An overview of the literature for 2005 is attempted to highlight works of interest and novelty and draw attention to those works which it is felt have provided a route to better analysis and increased the ability to understand the meaning of thermodynamic change on binding.
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Signaling through C2 domains: more than one lipid target.
TL;DR: This review summarizes the main structural and functional findings on Ca(2+) and lipid interactions by C2 domains, including the discovery of the phosphoinositide-binding site located in the β3-β4 strands.
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The Ca2+ Affinity of Synaptotagmin 1 Is Markedly Increased by a Specific Interaction of Its C2B Domain with Phosphatidylinositol 4,5-Bisphosphate
TL;DR: The data demonstrate that the acidic phospholipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), but not phosph atidylserine, markedly increases the calcium sensitivity of synaptotagmin, and lend support to the view that synaptoagmin functions by binding in a trans configuration.
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The annexins: spatial and temporal coordination of signaling events during cellular stress
TL;DR: The latest data on how changes in Ca2+ and pH homeostasis are sensed by annexins are reviewed, which have the ability to simultaneously interact with specific lipid and protein moieties at the plasma membrane, contributing to stress adaptation via regulation of various signaling pathways.
Journal ArticleDOI
Phosphatidylinositol 4,5-bisphosphate increases Ca2+ affinity of synaptotagmin-1 by 40-fold
TL;DR: Microscale thermophoresis shows that PIP2 binding to the polybasic patch of synaptotagmin-1 increases the Ca2+ affinity by >40-fold, which shows that this interplay between Ca2+, synaptolipid phosphatidylinositol 4,5-bisphosphate, and PIP1 is crucial for neurotransmitter release.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
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Protein kinase C and lipid signaling for sustained cellular responses.
TL;DR: It is now becoming evident that stimulation of a cell surface receptor initiates a degradation cascade of various membrane lipid constituents that has potentials to induce, intensify, and prolong the activation of protein kinase C that is needed for sustained cellular responses.
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Phosphoinositides in cell regulation and membrane dynamics
TL;DR: Inositol phospholipids mediate acute responses, but also act as constitutive signals that help define organelle identity, and play a fundamental part in controlling membrane–cytosol interfaces.
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Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells.
TL;DR: Fluorescence resonance energy transfer measurements in living cells revealed that acyl but not prenyl modifications promote clustering in lipid rafts, and the nature of the lipid anchor on a protein is sufficient to determine submicroscopic localization within the plasma membrane.