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

Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.

Molecular biology of the cell - 1 Dec 2011

Pais June E, Schilke Brenda, Craig Elizabeth A

Abstract excerpt

The heat-shock protein 70 (Hsp70)-based import motor, associated with the translocon on the matrix side of the mitochondrial inner membrane, drives translocation of proteins via cycles of binding and release. Stimulation of Hsp70's ATPase activity by the translocon-associated J-protein Pam18 is critical for this process. Pam18 forms a heterodimer with the structurally related protein Pam16, via their J-type...

Read the complete abstract on PubMed

Topics

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

Share to HSP70 Heat-Shock Proteins
Share to Membrane Transport Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Protein Multimerization

Share to Protein Transport

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22031295
DOI: 10.1091/mbc.E11-08-0715
PMCID: PMC3237618

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

Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor.PMID 22031295Read ↗

Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.Semantic proximity Read ↗

Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane.Semantic proximity Read ↗

Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.Semantic proximity Read ↗

Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.Semantic proximity Read ↗

Expansion of the evolutionarily conserved network of J-domain proteins in the Arabidopsis mitochondrial import complex.Semantic proximity Read ↗

Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.Semantic proximity Read ↗

Role of Magmas in protein transport and human mitochondria biogenesis.Semantic proximity Read ↗

Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import.Semantic proximity Read ↗

Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.Semantic proximity Read ↗

Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.Semantic proximity Read ↗

Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70.Semantic proximity Read ↗

Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane.Semantic proximity Read ↗

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