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

Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis.

Cell stress & chaperones - 1 Nov 2011

Murphy Lindsey A, Ramirez Emily A, Trinh Van T, Herman Alexander M, Anderson Valen C, Brewster Jay L

Abstract excerpt

FKBP65 is an endoplasmic reticulum (ER)-localized chaperone and rotamase, with cargo proteins that include tropoelastin and collagen. In humans, mutations in FKBP65 have recently been shown to cause a form of osteogenesis imperfecta (OI), a brittle bone disease resulting from deficient secretion of mature type I collagen. In this work, we describe the rapid proteolysis of FKBP65 in response to ER stress signals...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to EF Hand Motifs

Share to Endoplasmic Reticulum Stress

Share to Mutagenesis, Site-Directed

Share to Proteasome Endopeptidase Complex

Share to Proteolysis

Share to Tacrolimus Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 21761186
DOI: 10.1007/s12192-011-0270-x
PMCID: PMC3220392

Genes

DBI

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis.PMID 21761186Read ↗

Endoplasmic reticulum stress in the pathogenesis of fibrotic diseaseSemantic proximity Read ↗

Developmental Regulation of FKBP65Semantic proximity Read ↗

Interaction between KDELR2 and HSP47 as a Key Determinant in Osteogenesis Imperfecta Caused by Bi-allelic Variants in KDELR2.Semantic proximity Read ↗

Mutant MESD links cellular stress to type I collagen aggregation in osteogenesis imperfecta type XX.Semantic proximity Read ↗

Heat shock protein 47 and 65-kDa FK506-binding protein weakly but synergistically interact during collagen folding in the endoplasmic reticulum.Semantic proximity Read ↗

A Chaperone Complex Formed by HSP47, FKBP65, and BiP Modulates Telopeptide Lysyl Hydroxylation of Type I Procollagen.Semantic proximity Read ↗

Mechanisms and models of endoplasmic reticulum stress in chondrodysplasia.Semantic proximity Read ↗

Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta.Semantic proximity Read ↗

Osteoblast Malfunction Caused by Cell Stress Response to Procollagen Misfolding in α2(I)-G610C Mouse Model of Osteogenesis Imperfecta.Semantic proximity Read ↗

XBP1s-Mediated ER Proteostasis Network Enhancement Can Selectively Improve the Folding and Secretion of an Osteogenesis Imperfecta-Causing Collagen-I VariantSemantic proximity Read ↗

4-PBA ameliorates cellular homeostasis in fibroblasts from osteogenesis imperfecta patients by enhancing autophagy and stimulating protein secretion.Semantic proximity Read ↗

PERK Signaling Regulates Extracellular Proteostasis of an Amyloidogenic Protein During Endoplasmic Reticulum StressSemantic proximity Read ↗

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