The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization. - Wikidata - awgldk - TriplyDB

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

http://www.wikidata.org/entity/Q34926498

about

CARTS biogenesis requires VAP-lipid transfer protein complexes functioning at the endoplasmic reticulum-Golgi interface.Phosphoregulatory protein 14-3-3 facilitates SAC1 transport from the endoplasmic reticulum.SAC-1 ensures epithelial endocytic recycling by restricting ARF-6 activity.

P2860

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P2860

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

http://www.wikidata.org/entity/Q34926498

description

2013 nî lūn-bûn

@nan

2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@ast

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@en

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@nl

type

label

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@ast

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@en

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@nl

prefLabel

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@ast

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@en

The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@nl

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JOURNAL.PONE.0071112

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The first transmembrane domain of lipid phosphatase SAC1 promotes Golgi localization.

@en

P2093

Caroline A Enns

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

Jinzhi Wang

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

Juxing Chen

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

Peter Mayinger

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

P2860

The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex

Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins

GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch and shape the Golgi to promote budding

An investigation of the role of transmembrane domains in Golgi protein retention

Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function

Local control of phosphatidylinositol 4-phosphate signaling in the Golgi apparatus by Vps74 and Sac1 phosphoinositide phosphatase

Retention of the yeast Sac1p phosphatase in the endoplasmic reticulum causes distinct changes in cellular phosphoinositide levels and stimulates microsomal ATP transport.

SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast.

Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites.

Growth control of Golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase.

P304

e71112

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scholarly article

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8

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23936490

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P921

transmembrane protein

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3731292

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