Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex.

The Journal of biological chemistry - 26 Dec 2003

Rohde Holger M, Cheong Fei Ying, Konrad Gerlinde, Paiha Karin, Mayinger Peter, Boehmelt Guido

Abstract excerpt

The Saccharomyces cerevisiae SAC1 gene encodes an integral membrane protein of the endoplasmic reticulum (ER) and the Golgi apparatus. Yeast SAC1 mutants display a wide array of phenotypes including inositol auxotrophy, cold sensitivity, secretory defects, disturbed ATP transport into the ER, or suppression of actin gene mutations. At present, it is not clear how these phenotypes relate to the finding that SAC1...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Coatomer Protein
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Golgi Apparatus

Share to Lipid Metabolism

Share to Luminescent Proteins

Share to Phosphoric Monoester Hydrolases

Share to Schizosaccharomyces

Source

Identifiers

PMID: 14527956
DOI: 10.1074/jbc.M307983200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex.PMID 14527956Read ↗

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

Functional characterization of a mammalian Sac1 and mutants exhibiting substrate-specific defects in phosphoinositide phosphatase activity.Semantic proximity Read ↗

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

Crystal structure of the yeast Sac1: implications for its phosphoinositide phosphatase function.Semantic proximity Read ↗

The Sac1 phosphoinositide phosphatase regulates Golgi membrane morphology and mitotic spindle organization in mammals.Semantic proximity Read ↗

Regulation of intracellular phosphatidylinositol-4-phosphate by the Sac1 lipid phosphatase.Semantic proximity Read ↗

Three SAC1-like genes show overlapping patterns of expression in Arabidopsis but are remarkably silent during embryo development.Semantic proximity Read ↗

Cell growth-dependent coordination of lipid signaling and glycosylation is mediated by interactions between Sac1p and Dpm1p.Semantic proximity Read ↗

Assembly, organization, and function of the COPII coatSemantic proximity Read ↗

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

The yeast phosphatidylinositol-4-OH kinase pik1 regulates secretion at the Golgi.Semantic proximity Read ↗

Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.