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

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

Proceedings of the National Academy of Sciences of the United States of America - 30 Aug 2005

D'Silva Patrick R, Schilke Brenda, Walter William, Craig Elizabeth A

Abstract excerpt

Translocation of proteins across the mitochondrial inner membrane is an essential process requiring an import motor having mitochondrial Hsp70 (mtHsp70) at its core. The J protein partner of mtHsp70, Pam18, is an integral part of this motor, serving to stimulate the ATPase activity of mtHsp70. Pam16, an essential protein having an inactive J domain that is unable to stimulate mtHsp70's ATPase activity, forms a...

Read the complete abstract on PubMed

Topics

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

Share to Biological Transport, Active
Share to Calcium-Transporting ATPases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intracellular Membranes

Share to Mitochondrial Membrane Transport Proteins

Share to Mitochondrial Precursor Protein Import Complex Proteins

Share to Molecular Chaperones

Share to Molecular Motor Proteins

Share to Protein Structure, Quaternary

Source

Open in PubMed Open full text

Identifiers

PMID: 16105940
DOI: 10.1073/pnas.0505969102
PMCID: PMC1194952

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

Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.PMID 16105940Read ↗

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

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

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

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

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

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

The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.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 ↗

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

Mitochondrial AtPAM16 is required for plant survival and the negative regulation of plant immunity.Semantic proximity Read ↗

The yeast magmas ortholog pam16 has an essential function in fermentative growth that involves sphingolipid metabolism.Semantic proximity Read ↗

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