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 novel Golgi membrane protein is a partner of the ARF exchange factors Gea1p and Gea2p.

Molecular biology of the cell - 1 Jun 2003

Chantalat Sophie, Courbeyrette Régis, Senic-Matuglia Francesca, Jackson Catherine L, Goud Bruno, Peyroche Anne

Abstract excerpt

The Sec7 domain guanine nucleotide exchange factors (GEFs) for the GTPase ARF are highly conserved regulators of membrane dynamics and protein trafficking. The interactions of large ARF GEFs with cellular membranes for localization and/or activation are likely to participate in regulated recruitment of ARF and effectors. However, these interactions remain largely unknown. Here we characterize Gmh1p, the first...

Read the complete abstract on PubMed

Topics

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

Share to ADP-Ribosylation Factor 1
Share to ADP-Ribosylation Factors

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

Share to Endoplasmic Reticulum

Share to Golgi Apparatus

Share to Guanine Nucleotide Exchange Factors

Share to HeLa Cells

Share to Saccharomyces cerevisiae Proteins

Share to Yeasts

Source

Open in PubMed Open full text

Identifiers

PMID: 12808035
DOI: 10.1091/mbc.e02-10-0693
PMCID: PMC194885

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 novel Golgi membrane protein is a partner of the ARF exchange factors Gea1p and Gea2p.PMID 12808035Read ↗

The ARF exchange factors Gea1p and Gea2p regulate Golgi structure and function in yeast.Semantic proximity Read ↗

Functional diversification of closely related ARF-GEFs in protein secretion and recycling.Semantic proximity Read ↗

ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization.Semantic proximity Read ↗

AGD5 is a GTPase-activating protein at the trans-Golgi network.Semantic proximity Read ↗

Functional analysis of ADP-ribosylation factor (ARF) guanine nucleotide exchange factors Gea1p and Gea2p in yeast.Semantic proximity Read ↗

Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function.Semantic proximity Read ↗

The KDEL receptor regulates a GTPase-activating protein for ADP-ribosylation factor 1 by interacting with its non-catalytic domain.Semantic proximity Read ↗

Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors.Semantic proximity Read ↗

Emerging role of Cdc42-specific guanine nucleotide exchange factors as regulators of membrane trafficking in health and disease.Semantic proximity Read ↗

Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi apparatus.Semantic proximity Read ↗

Highly conserved motifs within the large Sec7 ARF guanine nucleotide exchange factor GBF1 target it to the Golgi and are critical for GBF1 activity.Semantic proximity Read ↗

Avl9 defines a family of GTPase-activating proteins that regulate diverse cell biological functionsSemantic proximity Read ↗

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