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

Features of membrane protein sequence direct post-translational insertion.

Nature communications - 25 Nov 2024

Kalinin Ilya A, Peled-Zehavi Hadas, Barshap Alon B D, Tamari Shai A, Weiss Yarden, Nevo Reinat, Fluman Nir

Abstract excerpt

The proper folding of multispanning membrane proteins (MPs) hinges on the accurate insertion of their transmembrane helices (TMs) into the membrane. Predominantly, TMs are inserted during protein translation, via a conserved mechanism centered around the Sec translocon. Our study reveals that the C-terminal TMs (cTMs) of numerous MPs across various organisms bypass this cotranslational route, necessitating an...

Read the complete abstract on PubMed

Topics

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

Share to Electron Transport Complex IV
Share to Escherichia coli Proteins

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

Share to Hydrophobic and Hydrophilic Interactions

Share to Membrane Transport Proteins

Share to Mitochondrial Proteins

Share to Protein Biosynthesis

Share to Protein Folding

Share to Protein Processing, Post-Translational

Source

Open in PubMed Open full text

Identifiers

PMID: 39587101
DOI: 10.1038/s41467-024-54575-6
PMCID: PMC11589881

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 17 Oct 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

Features of membrane protein sequence direct post-translational insertion.PMID 39587101Read ↗

Membrane protein sequence features direct post-translational insertionSemantic proximity Read ↗

An intramembrane chaperone complex facilitates membrane protein biogenesis.Semantic proximity Read ↗

The ER membrane complex (EMC) can functionally replace the Oxa1 insertase in mitochondria.Semantic proximity Read ↗

Role of a holo-insertase complex in the biogenesis of biophysically diverse ER membrane proteinsSemantic proximity Read ↗

Polarity and charge of the periplasmic loop determine the YidC and sec translocase requirement for the M13 procoat lep protein.Semantic proximity Read ↗

Mechanisms of multipass membrane protein biogenesisSemantic proximity Read ↗

Diversity and evolution of protein translocation.Semantic proximity Read ↗

The architecture of EMC reveals a path for membrane protein insertionSemantic proximity Read ↗

Triaging of α-helical proteins to the mitochondrial outer membrane by distinct chaperone machinery based on substrate topology.Semantic proximity Read ↗

Role of a holo-insertase complex in the biogenesis of biophysically diverse ER membrane proteinsSemantic proximity Read ↗

The Sec-independent function of Escherichia coli YidC is evolutionary-conserved and essential.Semantic proximity Read ↗

A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function.Semantic proximity Read ↗

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