Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions - Wikidata - wikimedia - TriplyDB

Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions

Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions

http://www.wikidata.org/entity/Q39583577

about

Synaptic vesicle recycling: steps and principles Organization and dynamics of SNARE proteins in the presynaptic membrane GLTP mediated non-vesicular GM1 transport between native membranes CaMKII binding to GluN2B is critical during memory consolidation Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.The extracellular δ-domain is essential for the formation of CD81 tetraspanin webs.Multi-protein assemblies underlie the mesoscale organization of the plasma membrane.Secretory vesicles are preferentially targeted to areas of low molecular SNARE density The reserve pool of synaptic vesicles acts as a buffer for proteins involved in synaptic vesicle recycling.Concentration Dependent Ion-Protein Interaction Patterns Underlying Protein Oligomerization Behaviours Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate.The yeast vacuolar ABC transporter Ybt1p regulates membrane fusion through Ca2+ transport modulation The Munc18-1 domain 3a hinge-loop controls syntaxin-1A nanodomain assembly and engagement with the SNARE complex during secretory vesicle priming.SNARE requirements en route to exocytosis: from many to few.Exocytosis through the Lens CaMKII: claiming center stage in postsynaptic function and organization.PI(4,5)P₂-binding effector proteins for vesicle exocytosis.The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions.No Evidence for Spontaneous Lipid Transfer at ER-PM Membrane Contact Sites.Oligomerization of the Tetraspanin CD81 via the Flexibility of Its δ-Loop Clustering of the K+ channel GORK of Arabidopsis parallels its gating by extracellular K+.Class C ABC transporters and Saccharomyces cerevisiae vacuole fusion The amyloid precursor protein forms plasmalemmal clusters via its pathogenic amyloid-β domain.Ca2+ regulates T-cell receptor activation by modulating the charge property of lipids.Introducing Membrane Charge and Membrane Potential to T Cell Signaling.Ca2+ controls gating of voltage-gated calcium channels by releasing the β2e subunit from the plasma membrane.

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P2860

Ca2+ induces clustering of membrane proteins in the plasma membrane via electrostatic interactions

http://www.wikidata.org/entity/Q39583577

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Ca2+ induces clustering of mem ...... via electrostatic interactions

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Ca2+ induces clustering of mem ...... ia electrostatic interactions.

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type

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Ca2+ induces clustering of mem ...... via electrostatic interactions

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Ca2+ induces clustering of mem ...... ia electrostatic interactions.

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Ca2+ induces clustering of mem ...... via electrostatic interactions

@en

Ca2+ induces clustering of mem ...... ia electrostatic interactions.

@nl

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P1433

The EMBO Journal

P1476

Ca2+ induces clustering of mem ...... via electrostatic interactions

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P2093

Arne Schreiber

http://www.w3.org/2001/XMLSchema#string

David Walrafen

http://www.w3.org/2001/XMLSchema#string

Felipe E Zilly

http://www.w3.org/2001/XMLSchema#string

Luis Spitta

http://www.w3.org/2001/XMLSchema#string

Nagaraj D Halemani

http://www.w3.org/2001/XMLSchema#string

Thorsten Lang

http://www.w3.org/2001/XMLSchema#string

P2860

Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes

Syntaxins 3 and 4 are concentrated in separate clusters on the plasma membrane before the establishment of cell polarity

Alternative splicing of SNAP-25 regulates secretion through nonconservative substitutions in the SNARE domain.

The challenge of lipid rafts

Membrane lipids: where they are and how they behave

Functional rafts in cell membranes

Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis

The fluid mosaic model of the structure of cell membranes

Characterization of the palmitoylation domain of SNAP-25

Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts

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1209-1220

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scholarly article

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10.1038/EMBOJ.2011.53

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7

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30

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2011-03-01T00:00:00Z

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50250449

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21364530

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3094119

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