An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels. - Wikidata - awgldk - TriplyDB

An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels.

An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels.

http://www.wikidata.org/entity/Q37744178

about

PI5P and PI(3,5)P2: Minor, but Essential Phosphoinositides.A copper-controlled RNA interference system for reversible silencing of target genes in Trichoderma reesei.Control of vacuole membrane homeostasis by a resident PI-3,5-kinase inhibitor.

P2860

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P2860

An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels.

http://www.wikidata.org/entity/Q37744178

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on February 2017

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@en

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@nl

type

label

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@en

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@nl

prefLabel

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@en

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@nl

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P356

MBC.E16-06-0390

P1433

Molecular Biology of the Cell

P1476

An intramolecular interaction ...... 3,5-bisphosphate lipid levels.

@en

P2093

Bethany S Strunk

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

Jason L Petersen

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

Lois S Weisman

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

Michael J Lang

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

Nadia Azad

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

P2860

VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse.

In vivo, Pikfyve generates PI(3,5)P2, which serves as both a signaling lipid and the major precursor for PI5P.

Assembly of a Fab1 phosphoinositide kinase signaling complex requires the Fig4 phosphoinositide phosphatase

The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover

Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes.

The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations

Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation

Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology.

Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p.

Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile.

P304

858-864

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scholarly article

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10.1091/MBC.E16-06-0390

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7

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28

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2017-02-01T00:00:00Z

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28148651

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5385934

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