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

A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.

Molecular biology of the cell - 1 Jul 1999

Coe J G, Lim A C, Xu J, Hong W

Abstract excerpt

Members of the syntaxin protein family participate in the docking-fusion step of several intracellular vesicular transport events. Tlg1p has been identified as a nonessential protein required for efficient endocytosis as well as the maintenance of normal levels of trans-Golgi network proteins. In this study we independently describe Tlg1p as an essential protein required for cell viability. Depletion of Tlg1p in...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Division
Share to Cloning, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 10397773
DOI: 10.1091/mbc.10.7.2407
PMCID: PMC25462

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae.PMID 10397773Read ↗

Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic.Semantic proximity Read ↗

The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport.Semantic proximity Read ↗

Two syntaxin homologues in the TGN/endosomal system of yeast.Semantic proximity Read ↗

Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteins.Semantic proximity Read ↗

Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Semantic proximity Read ↗

Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit.Semantic proximity Read ↗

Use1p is a yeast SNARE protein required for retrograde traffic to the ER.Semantic proximity Read ↗

Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex.Semantic proximity Read ↗

Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation.Semantic proximity Read ↗

LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum.Semantic proximity Read ↗

Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits both early Golgi function and ribosome biosynthesis.Semantic proximity Read ↗

Establishing a role for the GTPase Ypt1p at the late Golgi.Semantic proximity Read ↗

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