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

Function and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPase.

The Journal of biological chemistry - 11 Jul 2008

Qi Jie, Forgac Michael

Abstract excerpt

The vacuolar (H+)-ATPases (V-ATPases) are ATP-dependent proton pumps that operate by a rotary mechanism in which ATP hydrolysis drives rotation of a ring of proteolipid subunits relative to subunit a within the integral V(0) domain. In vivo dissociation of the V-ATPase (an important regulatory mechanism) generates a V(0) domain that does not passively conduct protons. EM analysis indicates that the N-terminal...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Factor Xa
Share to Ion Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nitrates

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Saccharomyces cerevisiae

Share to Vacuolar Proton-Translocating ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 18492665
DOI: 10.1074/jbc.M802442200
PMCID: PMC2443644

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Function and subunit interactions of the N-terminal domain of subunit a (Vph1p) of the yeast V-ATPase.PMID 18492665Read ↗

Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain.Semantic proximity Read ↗

The tether connecting cytosolic (N terminus) and membrane (C terminus) domains of yeast V-ATPase subunit a (Vph1) is required for assembly of V0 subunit d.Semantic proximity Read ↗

Analysis of the membrane topology of transmembrane segments in the C-terminal hydrophobic domain of the yeast vacuolar ATPase subunit a (Vph1p) by chemical modification.Semantic proximity Read ↗

The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H(+)-ATPase.Semantic proximity Read ↗

Mutational analysis of the catalytic subunit of the yeast vacuolar proton-translocating ATPase.Semantic proximity Read ↗

Some assembly required: Contributions of Tom Stevens' lab to the V-ATPase field.Semantic proximity Read ↗

Close-up and genomic views of the yeast vacuolar H+-ATPase.Semantic proximity Read ↗

TM2 but not TM4 of subunit c'' interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking.Semantic proximity Read ↗

Assembly of the yeast vacuolar H+-ATPase and ATP hydrolysis occurs in the absence of subunit c''.Semantic proximity Read ↗

Mutational analysis of subunit G (Vma10p) of the yeast vacuolar H+-ATPase.Semantic proximity Read ↗

Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump.Semantic proximity Read ↗

The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex.Semantic proximity Read ↗

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